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Information on EC 3.4.24.B20 - FtsH protease
for references in articles please use BRENDA:EC3.4.24.B20
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.B20 FtsH protease
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 3.4.24.B20
- chloroplast
-
photosystem
- thylakoids
-
variegation
-
photodamaged
-
photoinhibition
- sigma32
-
ftsh-mediated
- rpoh
-
grana
- lpxc
-
photoinhibitory
-
ftsh-dependent
showSynonyms
ftsh protease, ftsh2, ftsh1, ftsh11, ftsh5, ftsh3, ftsh6, ftsh12, atp-dependent zinc metalloprotease, atftsh2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
filamentation temperature sensitive H
filamentation temperature sensitive H protease
filamentation temperature-sensitive H
FtsH
FtsH1
FtsH10
FtsH11
FtsH12
FtsH2
FtsH3
FtsH4
FtsH5
FtsH6
FtsH8
HflB
M41.005
putative cell division protein
slr0228
-
is implicated in the repair of photodamaged photosystem II complexes
VAR2
zinc dependent protease
ZmFtsH2A
ZmFtsH2B
additional information
filamentation temperature sensitive H
-
FtsH6
gene expression is heat-inducible and rapidly responsive to heat stress
additional information
-
FtsH protease belongs to the ATP-dependent AAA+ protein family
additional information
the enzyme belongs to the AAA+ protease family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
degradative cleavage of proteins
-
-
-
-
degradative cleavage of proteins
specific for chloroplastic membrane proteins
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
253850-13-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-casein + H2O
?
-
Substrates: ATP is required for the reaction. The enzyme is unable to degrade the substrate in the presence of AMPPNP
Products: -
Products: -
?
EX1 + H2O
?
Substrates: substrate chloroplast protein EXECUTER1, involved in signaling by singlet oxygen
Products: -
Products: -
?
Fur repressor protein + H2O
?
Substrates: degraded by the FtsH1/FtsH3 complex
Products: -
Products: -
?
H+-ATPase F0alpha + H2O
?
-
Substrates: membrane substrate of FtsH
Products: -
Products: -
?
heat shock transcription factor sigma 32 + H2O
?
-
Substrates: -
Products: -
Products: -
?
IsiA chlorophyll-binding protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
light-harvesting chlorophyll a/b binding-green fluorescent protein + H2O
degraded light-harvesting chlorophyll a/b binding-green fluorescent protein + ?
-
Substrates: -
Products: -
Products: -
?
light-harvesting complex II + H2O
?
-
Substrates: AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
Products: -
Products: -
?
membrane-bound transcription factor of Staphylococcus aureus MbtS + H2O
?
-
Substrates: -
Products: -
Products: -
?
photosystem II reaction center protein D1 + H2O
?
-
Substrates: tryptophan oxidation at the N-terminus of D1 leads to processive degradation by the enzyme
Products: -
Products: -
?
photosystem II reaction center subunit D2 + H2O
?
-
Substrates: FtsH has a key role in the repair of UVB-damaged photosystem II
Products: -
Products: -
?
photosystem II subunit D1 + H2O
?
Substrates: -
Products: -
Products: -
?
photosystem II subunit D2 + H2O
?
Substrates: -
Products: -
Products: -
?
PsaA subunit of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
PsaB subunit of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
reaction center D1 protein + H2O
23-kDa N-terminal fragments of reaction center D1 protein
-
Substrates: -
Products: -
Products: -
?
Rieske FeS protein + H2O
?
-
Substrates: degradation of membrane protein, essentially required as a membrane-integrated quality control
Products: -
Products: -
?
subunit SecY of the SecAEG translocase + H2O
?
-
Substrates: membrane substrate of FtsH
Products: -
Products: -
?
unassembled Rieske FeS protein + H2O
?
-
Substrates: recombinant wild-type protein and mutant C162S, recombinant protein substrate is imported in vitro into intact Pisum sativum chloroplasts
Products: -
Products: -
?
Ycf37 assembly factor of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
Ycf4 assembly factor of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
Substrates: enzyme is required for protection against photoinhibition and induction of repair of photosystem II D1 protein, degradation of irreversible damaged D1 protein in form of the 23 kDa fragment
Products: -
Products: -
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
Substrates: irreversibly damaged substrate by reactive oxygen species formed in the light
Products: -
Products: -
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
Substrates: degradation, irreversibly damaged substrate by reactive oxygen species formed in the light
Products: -
Products: -
?
Anabaena apoflavodoxin + H2O
?
-
Substrates: FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
Products: -
Products: -
?
Anabaena apoflavodoxin + H2O
?
-
Substrates: FtsH degradation of 31 point mutants of Anabaena apoflavodoxin from Anabaena PCC 7119 is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form
Products: -
Products: -
?
casein + H2O
?
Substrates: artificial resorufin-labeled substrate
Products: -
Products: -
?
D1 protein + H2O
?
-
Substrates: FtsH protease is responsible for the primary cleavage of the D1 protein under moderate heat stress conditions
Products: -
Products: -
?
D1 protein + H2O
?
Substrates: substrate for isoform FtsH2
Products: -
Products: -
?
D1 protein + H2O
?
Substrates: isoform FtsH2 is involved in selective D1 protein degradation during photosystem II repair
Products: -
Products: -
?
damaged PSII D1 protein + H2O
?
Substrates: -
Products: -
Products: -
?
HflC + H2O
?
-
Substrates: substrate of both isoforms FtsH1 and FtsH2
Products: -
Products: -
?
HflC + H2O
?
-
Substrates: substrate of both isoforms FtsH1 and FtsH2
Products: -
Products: -
?
lambdaCII + H2O
?
-
Substrates: the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
Products: -
Products: -
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
?
photodamaged D1 protein + H2O
?
Substrates: degradation, part of photosystem 2 repair
Products: -
Products: -
?
photodamaged D1 protein + H2O
?
Substrates: degradation
Products: -
Products: -
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
?
photosystem II reaction center subunit D1 + H2O
?
-
Substrates: FtsH has a key role in the repair of UVB-damaged photosystem II
Products: -
Products: -
?
photosystem II reaction center subunit D1 + H2O
?
-
Substrates: -
Products: -
Products: -
?
PhzC + H2O
?
-
Substrates: substrate is a phenazine biosynthesis protein, and substrate of isoform FtsH1
Products: -
Products: -
?
PhzC + H2O
?
-
Substrates: substrate is a phenazine biosynthesis protein, and substrate of isoform FtsH1
Products: -
Products: -
?
PhzC + H2O
?
-
Substrates: substrate of isoform FtsH1
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II from photoinhibition, and the formation of thylakoids
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: FtsH11 protease plays a critical role in Arabidopsis thermotolerance. FtsH11 constitutively protects the photosynthesis apparatus from the damage caused by elevated temperatures
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: thylakoid FtsH protease is involved in the degradation of unassembled proteins, and in the turnover of the D1 protein of the PSII reaction center in the context of its repair from photoinhibition. FtsH proteases are involved in the formation of thylakoids
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: FtsH (slr0228) plays an important role in controlling the removal of unassembled PSII subunits from the thylakoid membrane
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: FtsH mediates repair of the photosystem II complex in response to light stress
Products: -
Products: -
?
protein + H2O
peptides
-
Substrates: unfoldase activity might be a common property of ATP-dependent proteases
Products: -
Products: -
?
protein + H2O
peptides
-
Substrates: degradation of membrane proteins, essentially required as a membrane-integrated quality control
Products: -
Products: -
?
protein + H2O
peptides
Substrates: degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
Products: -
Products: -
?
protein + H2O
peptides
Substrates: enzyme is involved in chloroplast biogenesis
Products: -
Products: -
?
protein + H2O
peptides
-
Substrates: degradation of unassembled proteins, apoproteins lacking their prostethic groups or pigments, photo-or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
Products: -
Products: -
?
protein + H2O
peptides
-
Substrates: degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
Products: -
Products: -
?
protein D1 + H2O
?
-
Substrates: FtsH (slr0228) is required for selective D1 turnover during photosystem II repair
Products: -
Products: -
?
protein D1 + H2O
?
-
Substrates: FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions
Products: -
Products: -
?
RNase colicin D + H2O
?
-
Substrates: the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
Products: -
Products: -
?
RNase colicin D + H2O
?
-
Substrates: the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
Products: -
Products: -
?
RpoH + H2O
?
-
Substrates: RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
Products: -
Products: -
?
RpoH + H2O
?
-
Substrates: several RpoH residues critical for degradation are located in the highly conserved region 2.1. The double mutation A131E/K134V significantly stabilizes RpoH against degradation by the FtsH protease, while the single-point mutations at these positions only show a slight effect on RpoH stability. A minimal RpoH variant composed of residues L37-G147, including region 2.1 and C, is a sufficient FtsH substrate. Region 2.1 and region C might serve as interaction surfaces for FtsH-mediated degradation
Products: -
Products: -
?
RpoH + H2O
?
-
Substrates: substrate heat shock transcription factor RpoH is degraded rapidly in the wild-type and FtsH2 deletion mutant background with a half-life of less than 10 min, and degraded with an estimated half-life between 10 and 30 min in the FtsH1 mutant and FtsH1 FtsH2 double mutant background
Products: -
Products: -
?
RpoH + H2O
?
-
Substrates: major substrate of isoform FtsH1
Products: -
Products: -
?
RpoH + H2O
?
-
Substrates: substrate heat shock transcription factor RpoH is degraded rapidly in the wild-type and FtsH2 deletion mutant background with a half-life of less than 10 min, and degraded with an estimated half-life between 10 and 30 min in the FtsH1 mutant and FtsH1 FtsH2 double mutant background
Products: -
Products: -
?
RpoH + H2O
?
-
Substrates: major substrate of isoform FtsH1
Products: -
Products: -
?
Spo0E + H2O
?
-
Substrates: the Spo0E phosphatase is distinguished from the YisI and YnzD phosphatases by a C-terminal extension of about 25 amino acids, the C-terminal region of Spo0E confers target specificity to FtsH
Products: -
Products: -
?
additional information
?
-
-
Substrates: the D1 protein, a core subunit of the PSII reaction enter, is a substrate for FtsH protease
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme forms a heteromeric complex with inactive FtsH subunits and plastid NAD-malate dehydrogenase
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme does not associate with FTSH7, FTSH9, FTSH12, nor FTSHi1-4
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme does not associate with FTSH7, FTSH9, FTSH12, nor FTSHi1-4
Products: -
Products: -
-
additional information
?
-
-
Substrates: neither phosphatases YisI nor YnzD, homologues of Spo0E, are substrates of FtsH
Products: -
Products: -
?
additional information
?
-
-
Substrates: CYN28 interacts with the enzyme complexes on the thylakoid lumen side and is involved in enzyme turnover under high light stress
Products: -
Products: -
-
additional information
?
-
Chlamydomonas reinhardtii cc5325
-
Substrates: CYN28 interacts with the enzyme complexes on the thylakoid lumen side and is involved in enzyme turnover under high light stress
Products: -
Products: -
-
additional information
?
-
-
Substrates: the six AAA domains bind and translocate proteins that are targeted for destruction in an ATP-dependent manner into the interior of the molecule, where the proteolytic sites are located and where substrate proteins are degraded in a processive manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
Substrates: FtsH is complexed with HflCK
Products: -
Products: -
?
additional information
?
-
-
Substrates: complex substrate recognition mechanisms, detailed overview. The ATPase domain forms the entrance to the central pore of FtsH with a diameter of about 15 A, a conserved Phe at position 228 of the pore is crucial for substrate binding. Substrates are pulled through the narrow gate and into the following protease domain using the energy of ATP hydrolysis for unfolding and translocation of the proteins. FtsH has only weak unfolding activity and is not able to degrade tightly folded model substrate proteins like GFP or DHFR
Products: -
Products: -
?
additional information
?
-
-
Substrates: mutational substrate analysis, structure-function anaylsis, modelling, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with GST and bovine serum albumin
Products: -
Products: -
?
additional information
?
-
-
Substrates: the membrane protein SrtA is not a substrate
Products: -
Products: -
-
additional information
?
-
Substrates: the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
Products: -
Products: -
?
additional information
?
-
-
Substrates: the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
Products: -
Products: -
?
additional information
?
-
Substrates: photosystem II subunits CP47 and CP43 are much more resistant to proteolytic degradation in the dark than subunit D1 and D2
Products: -
Products: -
?
additional information
?
-
Substrates: an active-site switch is formed by a substrate-binding beta-strand
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Anabaena apoflavodoxin + H2O
?
-
Substrates: FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
Products: -
Products: -
?
Fur repressor protein + H2O
?
Substrates: degraded by the FtsH1/FtsH3 complex
Products: -
Products: -
?
heat shock transcription factor sigma 32 + H2O
?
-
Substrates: -
Products: -
Products: -
?
IsiA chlorophyll-binding protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
lambdaCII + H2O
?
-
Substrates: the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
Products: -
Products: -
?
light-harvesting complex II + H2O
?
-
Substrates: AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
Products: -
Products: -
?
photosystem II reaction center protein D1 + H2O
?
-
Substrates: tryptophan oxidation at the N-terminus of D1 leads to processive degradation by the enzyme
Products: -
Products: -
?
PsaA subunit of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
PsaB subunit of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
Rieske FeS protein + H2O
?
-
Substrates: degradation of membrane protein, essentially required as a membrane-integrated quality control
Products: -
Products: -
?
Spo0E + H2O
?
-
Substrates: the Spo0E phosphatase is distinguished from the YisI and YnzD phosphatases by a C-terminal extension of about 25 amino acids, the C-terminal region of Spo0E confers target specificity to FtsH
Products: -
Products: -
?
Ycf37 assembly factor of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
Ycf4 assembly factor of photosystem I + H2O
?
-
Substrates: -
Products: -
Products: -
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
Substrates: enzyme is required for protection against photoinhibition and induction of repair of photosystem II D1 protein, degradation of irreversible damaged D1 protein in form of the 23 kDa fragment
Products: -
Products: -
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
Substrates: degradation, irreversibly damaged substrate by reactive oxygen species formed in the light
Products: -
Products: -
?
D1 protein + H2O
?
-
Substrates: FtsH protease is responsible for the primary cleavage of the D1 protein under moderate heat stress conditions
Products: -
Products: -
?
D1 protein + H2O
?
Substrates: substrate for isoform FtsH2
Products: -
Products: -
?
D1 protein + H2O
?
Substrates: isoform FtsH2 is involved in selective D1 protein degradation during photosystem II repair
Products: -
Products: -
?
damaged PSII D1 protein + H2O
?
Substrates: -
Products: -
Products: -
?
HflC + H2O
?
-
Substrates: substrate of both isoforms FtsH1 and FtsH2
Products: -
Products: -
?
HflC + H2O
?
-
Substrates: substrate of both isoforms FtsH1 and FtsH2
Products: -
Products: -
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
?
photodamaged D1 protein + H2O
?
Substrates: degradation, part of photosystem 2 repair
Products: -
Products: -
?
photodamaged D1 protein + H2O
?
-
Substrates: -
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
Products: the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
?
PhzC + H2O
?
-
Substrates: substrate of isoform FtsH1
Products: -
Products: -
?
Protein + H2O
?
-
Substrates: FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II from photoinhibition, and the formation of thylakoids
Products: -
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Protein + H2O
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Substrates: FtsH11 protease plays a critical role in Arabidopsis thermotolerance. FtsH11 constitutively protects the photosynthesis apparatus from the damage caused by elevated temperatures
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Protein + H2O
?
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Substrates: thylakoid FtsH protease is involved in the degradation of unassembled proteins, and in the turnover of the D1 protein of the PSII reaction center in the context of its repair from photoinhibition. FtsH proteases are involved in the formation of thylakoids
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Protein + H2O
?
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Substrates: FtsH (slr0228) plays an important role in controlling the removal of unassembled PSII subunits from the thylakoid membrane
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Protein + H2O
?
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Substrates: FtsH mediates repair of the photosystem II complex in response to light stress
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protein + H2O
peptides
-
Substrates: degradation of membrane proteins, essentially required as a membrane-integrated quality control
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protein + H2O
peptides
Substrates: degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
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protein + H2O
peptides
Substrates: enzyme is involved in chloroplast biogenesis
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protein + H2O
peptides
-
Substrates: degradation of unassembled proteins, apoproteins lacking their prostethic groups or pigments, photo-or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
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protein + H2O
peptides
-
Substrates: degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
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protein D1 + H2O
?
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Substrates: FtsH (slr0228) is required for selective D1 turnover during photosystem II repair
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protein D1 + H2O
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Substrates: FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions
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RNase colicin D + H2O
?
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Substrates: the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
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RNase colicin D + H2O
?
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Substrates: the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
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RpoH + H2O
?
-
Substrates: RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
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RpoH + H2O
?
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Substrates: major substrate of isoform FtsH1
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RpoH + H2O
?
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Substrates: major substrate of isoform FtsH1
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additional information
?
-
-
Substrates: the D1 protein, a core subunit of the PSII reaction enter, is a substrate for FtsH protease
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additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
Products: -
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?
additional information
?
-
Substrates: the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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additional information
?
-
-
Substrates: the six AAA domains bind and translocate proteins that are targeted for destruction in an ATP-dependent manner into the interior of the molecule, where the proteolytic sites are located and where substrate proteins are degraded in a processive manner
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additional information
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Substrates: fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview
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additional information
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-
Substrates: FtsH is complexed with HflCK
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additional information
?
-
Substrates: the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
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additional information
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-
-
Substrates: the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
ATP binding is not necessary for enzyme assembly, enzyme contains conserved Walker-type ATPase domain of approximately 230 amino acids, dependent on
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
additional information
Zn2+
dependent on
Zn2+
required
Zn2+
required, Var2 contains a Zn-binding site, HEXXH, in their protease domain
Zn2+
-
dependent on. FtsH is a metalloprotease and the protease domain contains the zinc-coordinating HEXXH motif
additional information
-
Mg2+ cannot substitute for the required divalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HflC protein
-
purified recombinant His6-tagged, 74 kDa dimers from Escherichia coli expressed in strain Bl21, inhibits the proteolysis of lambdaCII by FtsH, i.e. HflB, both in vitro and in vivo, mechanism, overview. Each HflC molecules interacts with another HflC molecule attached to the juxtaposed HflB
-
HflK protein
-
purified recombinant His6-tagged, 74 kDa dimers from Escherichia coli expressed in strain Bl21, inhibits the proteolysis of lambdaCII by FtsH, i.e. HflB, both in vitro and in vivo, mechanism, overview. Each HflK molecules interacts with another HflK molecule attached to the juxtaposed HflB
-
additional information
-
no inhibition by serine and cysteine protease inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
dependent on
ATP
dependent on
ATP
dependent on, Var2 contains an ATP-binding site, the second region of homology or SRH domain
ATP
-
dependent on, the C-terminus comprise the cytoplasmic ATPase and protease domain. The ATPase domain contains the Walker A/B motifs and the second region of homology responsible for the binding and hydrolysis of ATP
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Albinism
Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis.
Arthritis, Rheumatoid
Cheminformatics-based drug design approach for identification of inhibitors targeting the characteristic residues of MMP-13 hemopexin domain.
ftsh protease deficiency
Impaired PSII proteostasis triggers a UPR-like response in the var2 mutant of Arabidopsis.
Infections
A single amino acid of a Salmonella virulence protein contributes to pathogenicity by protecting from the FtsH-mediated proteolysis.
Iron Deficiencies
Two essential FtsH proteases control the level of the Fur repressor during iron deficiency in the cyanobacterium Synechocystis sp. PCC 6803.
Malaria
A single point mutation in the Plasmodium falciparum FtsH1 metalloprotease confers actinonin resistance.
Osteoarthritis
Cheminformatics-based drug design approach for identification of inhibitors targeting the characteristic residues of MMP-13 hemopexin domain.
Tetanus
Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells.
Tuberculosis
Cloning and expression of the gene coding for FtsH protease from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Functional characterization of AAA family FtsH protease of Mycobacterium tuberculosis.
Tuberculosis
Phosphorylation-dependent interaction between a serine/threonine kinase PknA and a putative cell division protein Wag31 in Mycobacterium tuberculosis.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.37
FtsH5, sequence calculation
5.64
FtsH1, sequence calculation
5.72
FtsH8, sequence calculation
5.8
FtsH11, sequence calculation
5.99
FtsH2, sequence calculation
6.49
FtsH12, sequence calculation
6.8
FtsH3, sequence calculation
7.21
FtsH6, sequence calculation
7.66
FtsH9, sequence calculation
8.3
FtsH7, sequence calculation
8.44
FtsH10, sequence calculation
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform FtsH3, predominantly expressed
UniProt
brenda
Q7V1V9 i.e. isoform FtsH1, and Q7V362, i.e. isoform Ftsh2, predominantly expressed isoforms
Q7V1V9; Q7V362
UniProt
brenda
Q7V1V9 i.e. isoform FtsH1, and Q7V362, i.e. isoform Ftsh2, predominantly expressed isoforms
Q7V1V9; Q7V362
UniProt
brenda
-
670551, 670555, 670563, 670580, 670676, 682278, 720304, 720686, 720706, 734540, 734854, 734984, 735051, 753707
-
-
brenda
cell division protease ftsH homolog 1, chloroplast precursor
SwissProt
brenda
ecotype Columbia. The var1 variegation mutant, which is defective in AtFtsH5, has coordinate reduction in the AtFtsH2 and 8 pair. The levels of both pairs are restired to normal in var1 plants that overexpress AtFtsH1
-
-
brenda
enzyme belongs to the AAA family of proteins, i.e. ATPases associated with diverse cellular activities
SwissProt
brenda
FtsH subunits are encoded by type-A (FtsH1 and FtsH5) and type-B (FtsH2 and FtsH8) genes
-
-
brenda
gene AtFtsH2 or var2; gene var2 variations, different mutated alleles, overview
SwissProt
brenda
strains SS120 and MIT9313, representing two ecotypes belonging to the low-light-adapted ecotype subclades II and IV, respectively
-
-
brenda
Q55700 i.e. isoform FtsH2, P72991 i.e. isoform FtsH3
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
brenda
additional information
-
FtsH is encoded by a family of 12 genes. Four of them, FtsH1, 2, 5, and 8 are found in chlorplast. Mutations in two of these, FTsH2 and 5, demonstrate a visible phenotype of variegated leaves. Transcription level in the FtsH2 mutant is higher than in the wild-type. FtsH protein level in the FtsH2 mutant is ca. 50% of that found in the wild-type
brenda
-
the most abundant FtsH isoenzyme is FtsH2, followed by FtsH5 and 8, with FtsH being accumulated to only 10% of FtsH2 level
brenda
-
brenda
-
brenda
additional information
-
AtStsH1, 2, 5, and 8 do not show evidence of tissue or developmental specific expression
brenda
additional information
-
quantitative real time RT-PCR expression analysis, and expression pattern under nutrient starvation, effects on expression levels of the ftsh genes, overview
brenda
additional information
semi-quantitative tissue-specific expression analysis of ZmFtsH2A in maize, overview
brenda
additional information
semi-quantitative tissue-specific expression analysis of ZmFtsH2A in maize, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoforms FtsH 7 and 9 are localized in the chloroplast envelope membrane
-
brenda
-
the enzyme is expressed in non-photosynthetic plastids, located in the inner envelope with its C-terminus exposed to the stroma
brenda
additional information
-
FtsH co-purifies with PSII complexes in Synechocystis
-
brenda
gene var2 expression influences the chloroplast structure
brenda
-
FtsH is encoded by a family of 12 genes. Four of them, FtsH1, 2, 5, and 8 are found in chloroplast. Mutations in two of these, FTsH2 and 5, demonstrate a visible phenotype of variegated leaves, with the phenotype of the FtsH2 mutant being more pronounced
brenda
-
thylakoid membrane, FtsH2 is the most abundant isomer, followed by FtsH5, FtsH8 and 1. Arabidopsis thalaina contains 12 genes encoding FtsH proteins, nine of them can be targeted to chloroplast, the other three are mitochondrial
brenda
-
FtsH comprises 12 members (AtFtsH1-AtFtsH12) including three pairs of closely related genes that are targeted to chloroplasts (AtFtsH2 and AtFtsH8, AtFtsH1 and AtFtsH5, AtFtsH7 and AtFtsH9)
brenda
-
FtsH2 and FtsH8, FtsH11 and FtsH5, FtsH7 and FtsH9 are closely related pairs. FtsH2 is the most abundant FtsH protein in chloroplast, followed by FtsH5. FtsH2 mutant has the most severe variegation and sensitivity to photoinhibition. The FtsH5 mutant shows similar, although much less pronounced, defects. FtsH8 and FtsH1 mutants behave like wild type plants. The overexpression of FtsH8 complements the FtsH2 mutant, and overexpression of FtsH1 complements the FtsH5 mutant. Thus, the genes within these closely related pairs are fully redundant
brenda
-
brenda
-
brenda
-
isoforms FtsH1, FtsH2, FtsH5, FtsH7, FtsH8, FtsH9, and FtsH11
brenda
-
isoforms FtsH1 and FtsH2 are the major isoforms comprising the FtsH complex in tobacco chloroplasts
brenda
FtsH1/FtsH3 complex
-
brenda
isoform FtsH1 is found mainly in the cytoplasmic membrane
-
brenda
-
hexamers of the FtsH proteases are localized near the Photosystem II complexes at the grana
brenda
-
hexamers of the FtsH proteases are localized near the Photosystem II complexes at the grana
brenda
-
hexamers of the FtsH proteases are localized near the Photosystem II complexes at the grana
brenda
-
the hexameric FtsH protease is anchored to the inner membrane by two transmembrane helices per monomer such that both termini protrude into the cytoplasm
brenda
-
Arabidopsis thalaina contains 12 genes encoding FtsH proteins, nine of them can be targeted to chloroplast, the other three are mitochondrial
brenda
-
brenda
-
brenda
exclusively, integral membrane protein, the hydrophilic part is exposed to the stroma of the chloroplast
brenda
protein is imported into isolated chloroplasts
brenda
-
brenda
-
brenda
VAR1 forms complexes with VAR2
brenda
-
the precursor of FtsH2 requires the proton gradient whereas the precursor of FtsH5 requires NTPs for thylakoid integration
brenda
-
isoforms FtsH 1, 2, 5 and 8 are localized in the thylakoid membrane
brenda
-
exclusively, integral membrane protein, the hydrophilic part is exposed to the stroma of the chloroplast
brenda
-
exclusively, integral membrane protein, the hydrophilic part is exposed to the stroma of the chloroplast
brenda
-
FtsH is found not only in the stroma thylakoids but also in the Photosystem II-enriched grana membranes (more abundant in the stroma thylakoids than in the grana)
brenda
-
-
brenda
isoform FtsH protein 4is found either in the thylakoid or at the interface between the thylakoid and cytoplasmic membranes
brenda
isoform FtsH protein 2 is found either in the thylakoid or at the interface between the thylakoid and cytoplasmic membranes
brenda
isoform FtsH protein 3 is found either in the thylakoid or at the interface between the thylakoid and cytoplasmic membranes
brenda
FtsH1/FtsH3 complex
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
FtsH gene multiplication is of adaptive value during the course of evolution of oxygenic photosynthesis
evolution
-
the mode of action of FtsH proteases seems to be different between cyanobacteria and higher plants
malfunction
-
mutants lacking isoforms FtsH2 and FtsH5 are characterized by a typical leaf-variegated phenotype
malfunction
a mutant depleted in isoform FtsH3 displays impaired protein D1 degradation
malfunction
-
the loss of isoform FtsH4 regulates Arabidopsis development and architecture by mediating the peroxidase-dependent interplay between hydrogen peroxide and auxin homeostasis
malfunction
A stabilizing effect on Fur is observed in a mutant conditionally depleted in the FtsH1 subunit
malfunction
a mutant conditionally depleted in FtsH3 is unable to induce normal expression of the IsiA chlorophyll-protein and FutA1 iron transporter upon iron deficiency due to a block in transcription, which is regulated by the Fur transcriptional repressor
malfunction
the ftsh1-1 mutation Increases photosystem II sensitivity to photoinhibition, prevents photosystem II repair, and leads to the accumulation of D1 protein fragments
malfunction
-
mutant seedlings with reduced enzyme abundance exhibit pale cotyledons and small, deformed chloroplasts with altered thylakoid structure. Mature plants retain these chloroplast defects, resulting in slightly variegated leaves and lower chlorophyll content. The strong changes in the proteome composition of FTSH12 knock-down seedlings reflect their impaired plastid development
malfunction
-
homozygous null mutants of the pseudo-proteases FtsHi1, 2, 4, 5 are embryo-lethal. Homozygous ftshi3 or a weak point mutant in FTSHi1 are affected in overall plant growth and development
metabolism
enzyme regulation, overview
metabolism
-
FtsH5/VAR1, FtsH2/VAR2, VAR3 and THF1 control leaf variegation in Arabidopsis thaliana
metabolism
-
FtsH cellular functions and regulation involving several factors, overview
metabolism
-
the thylakoid located FtsH complex in Arabidopsis is responsible for degradation of photodamaged D1 protein in concert with lumenal Deg proteases
physiological function
in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins
physiological function
-
FtsH has both chaperone and protease activities, and it is a crucial element in protein quality control, involving a number of substrates and processes, including the degradation of unneeded and damaged membrane proteins as well as soluble signaling factors
physiological function
-
in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins. slr0228 is involved in the early steps of D1 degradation and also plays a role in the removal of other damaged or unassembled thylakoid proteins
physiological function
-
FtsH is a peculiar prokaryotic protease with low unfoldase activity. FtsH takes care of degrading unstable or inappropriately assembled proteins
physiological function
-
FtsH has to degrade or to regulate the steady-state level of one or more proteins that interfere with successful sporulation. In the absence of the ATP-dependent metalloprotease FtsH, the sporulation frequency of Bacillus subtilis cells is reduced by several orders of magnitude
physiological function
-
the ATP-dependent metalloprotease FtsH is involved in the degradation of the photo- or heat-damaged D1 protein. Damage occurs in the reaction center-binding D1 protein understrong visible light and heat stress, overview
physiological function
-
the ATP-dependent zinc metallopeptidase is a cell division protein
physiological function
FtsH is a membrane-bound protein essential for the cell viability in Escherichia coli
physiological function
the ATP-dependent zinc metallopeptidase is a cell division protein
physiological function
the ATP-dependent zinc metallopeptidase is involved in the repair of PSII following damage incurred during photoinhibition. FtsH2 and FtsH5 are responsible for leaf variegation and proteolysis of photodamaged D1 protein in Arabidopsis
physiological function
the ATP-dependent zinc metallopeptidase is a cell division protein. FtsH2 and FtsH5 are responsible for leaf variegation and proteolysis of photodamaged D1 protein in Arabidopsis
physiological function
the ATP-dependent zinc metallopeptidase is involved in the degradation of both Lhcb3 and Lhcb1 during senescence and high-light acclimation
physiological function
the FtsH2 protease plays a key role in the degradation of both precursor and mature forms of D1 following donor-side photoinhibition, and in the selective degradation of photodamaged D1 protein and incompletely processed forms of the D1 protein during the repair of photosystem II in the cyanobacterium, overview. The FtsH2 protease participates in fast D1 replacement in the psbO deletion strain
physiological function
-
Chloroplast development promoted by the ectopic expression of cGPA1 is dependent on FtsH complexes. FtsH complexes, which are composed of type-A (FtsH1/FtsH5) and type-B (FtsH2/FtsH8) subunits, are required for cGPA1-promoted chloroplast development in the leaf-variegated mutant thylakoid formation 1, thf1, overview
physiological function
FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber
physiological function
-
FtsH is the only known membrane-anchored AAA protease in bacteria that fulfills a variety of regulatory functions. FtsH-mediated regulation of LpxC levels by proteolysis crucial for cell viability. FtsH is involved in the quality control of misfolded or incorrectly inserted membrane proteins and acts either as a chaperone to help them refold or degrades them. Another important function of FtsH in Escherichia coli is control of heat shock gene expression, overview
physiological function
-
FtsH is an essential membrane-bound protease that degrades integral membrane proteins as well as cytoplasmic proteins. FtsH is a stress-response protein that promotes the pathogen's ability to deal with reactive oxygen intermediates stress and is possibly involved in the regulation of FtsZ levels. Optimal intracellular levels of the essential cell-division protein FtsZ are critical for cell division and viability, overview
physiological function
VAR2, a subunit of the chloroplast FtsH complex, is involved in turnover of the photosystem II reaction center D1 protein, as well as in other processes required for the development and maintenance of the photosynthetic apparatus
physiological function
filamentation temperature-sensitive H, FtsH, is a membrane-anchored ATP-dependent metalloprotease
physiological function
in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins. The AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
physiological function
-
the heteromeric FtsH complex is important for maintaining thylakoid membranes
physiological function
-
part of the FtsH hexamers are juxtapositioned to PSII complexes in the grana in darkness, carrying out immediate degradation of the photodamaged D1 protein under light stress
physiological function
-
FtsH is necessary for the processing of colicinsDand E3 during their import
physiological function
-
interplay between N-terminal methionine excision and FtsH protease is essential for normal chloroplast development and function. The N-terminally processed D1 and D2 polypeptide chains are primarily degraded by the FtsH complex, which ensures their quality control
physiological function
isoform FtsH2 is involved in the repair of photosystem II within the thylakoid membranes
physiological function
FtsH metalloproteases are key components of the photosystem II repair cycle which operates to maintain photosynthetic activity in the light. isoforms FtsH1 and FtsH3 are required for cell viability, whereas FtsH2 and FtsH4 are dispensable. isoform FtsH3 is more important than FtsH2 for cell viability
physiological function
-
FtsH1 is a regulatory protein for organelle biogenesis in Plasmodium falciparum
physiological function
the FtsH1 protease is involved in the acclimation of cells to iron deficiency
physiological function
the FtsH2/FtsH3 complex is involved in photoprotection
physiological function
the FtsH2/FtsH3 complex is involved in photoprotection. The FtsH3 protease is involved in the acclimation of cells to iron deficiency
physiological function
FtsH is involved in quality control and the regulation of accumulation of cytochrome b6f complexes and complex C subunit B proteins. The enzyme regulates the degradation of photosystem II upon photoinhibition and phosphorus and sulfur starvation
physiological function
the proteolytic activity, and not only the ATPase one, is essential for conferring thermotolerance to the plants. FTSH11 interacts with different components of the CPN60 chaperonin. CPN60s as well as a number of envelope, stroma and thylakoid proteins are found associated with proteolytically inactive FTSH11. In a knockout strain, protein TIC40 is highly stabilized. The nucleotide antiporter PAPST2, the fatty acid binding protein FAP1 and the chaperone HSP70 are trapped in an affinity enrichment assay
physiological function
-
phylogenetic analysis of over 6000 FtsH protease sequences. The FtsH proteases involved in PSII repair form a distinct clade branching out before the divergence of FtsH proteases found in all groups of anoxygenic phototrophic bacteria. The phylogenetic tree of FtsH proteases in phototrophic bacteria is similar to that for Type I and Type II reaction centre proteins
physiological function
A8IL08; A8J6C7
upon high light exposure, the FtsH1 and FtsH2 and subunits display a shorter half-life, which is counterbalanced by an increase in FTSH1/2 mRNA levels, resulting in modest upregulation of FtsH1/2 proteins. High light increases the protease activity through a redox-controlled reduction of intermolecular disulfide bridges. In a FTSH1 promoter-deficient mutant, the abundance of FtsH1 and FtsH2 proteins are loosely coupled (decreased by 70% and 30%, respectively) with no formation of large and stable homo-oligomers. High light tolerance is tightly correlated with the abundance of the FtsH protease
physiological function
protein Psb29a minor component of His-tagged photosystem II preparations, physically interacts with FtsH complexes in vivo and is required for normal accumulation of the FtsH2/FtsH3 hetero-oligomeric complex involved in photosystem II repair. In a Psb29 null mutant, levels of FtsH2 and FtsH3 are substantially decreased
physiological function
FtsH is a highly dynamic protease undergoing sequential transitions between five conformational states on the second timescale. Addition of ATP does not influence the number of states or change the timescale of domain motions but affects the state occupancy distribution leading to an interdomain compaction
physiological function
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA. MIT 9313 has less of the FtsH protease
physiological function
Q7V1V9; Q7V362
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA
physiological function
-
deletion mutants of isoform FtsH1 display a severe growth retardation both in LB and M63 medium. The lag phase is extended from 6 to 8 h and retardation of growth at the second phase of the biphasic growth curve leads to a 1.5 h longer doubling time in the FtsH1 FtsH2 double mutant compared to the FtsH1 mutant. The FtsH2 mutant does not show a pronounced growth retardation phenotype. Deletion of FtsH1, but not FtsH2 moderately enhances sensitivity to a lethal heat shock. Deletion of FtsH1 causes a 13% reduction in swimming motility, which is 38% reduction the FtsH1 FtsH2 double deletion background. The FtsH1 mutant forms an undifferentiated flat biofilm. The FtsH1 FtsH2 double mutant forms dense irregular biofilm structures anchored to the substratum at a few contact points
physiological function
initiation of singlet oxygen signaling in grana margins depends on EX1 and the ATP-dependent zinc metalloprotease FtsH. FtsH cleaves also the D1 protein during the disassembly of damaged PSII, EX1-and singlet oxygen-mediated may be spatially but also functionally associated with the repair of PSII
physiological function
mutation of FtsH11 gene causes significant decreases in photosynthetic efficiency of photosystems when environmental temperature raises above optimal. Under moderately high temperatures, the FtsH11 mutant shows significant decreases in electron transfer rates of photosystem II (PSII) and photosystem I (PSI), decreases in photosynthetic capabilities of PSII and PSI, increases in non-photochemical quenching, and a host of other chlorophyll fluorescence parameter changes. For plants grown under normal temperature and subjected to the high light treatment, no significant difference in chlorophyll fluorescence parameters is found between the FtsH11 mutant and Col-0 WT plants
physiological function
-
the enzyme has highest impact during seedling development. Its abundance alters the plastid import machinery and impairs chloroplast development
physiological function
-
enzyme isoforms FtsH1 and FtsH2 contribute to motility and biofilm development, regulate pyoverdine and Pseudomonas quinolone signal production, and contribute to HOCl oxidative stress tolerance and aminoglycoside tolerance in planktonic culture and in biofilms of Pseudomonas aeruginosa. Isoform FtsH1 regulates autolysis
physiological function
-
the enzyme maintains protein quality in mitochondria and is involved in photosystem II repair
physiological function
the proteolytic activity of the enzyme, and not only its ATPase one, is essential for conferring thermotolerance in Arabidopsis. The enzyme is involved in regulating the level of the chloroplast import machinery at the inner envelope membrane
physiological function
-
the enzyme is required for the N-terminal degradation of LhcB2-GFP during de-etiolation
physiological function
-
the enzyme is involved in the degradation of photodamaged D1 during the photosystem II repair cycle
physiological function
-
FtsH is an essential membrane-bound protease that degrades integral membrane proteins as well as cytoplasmic proteins. FtsH is a stress-response protein that promotes the pathogen's ability to deal with reactive oxygen intermediates stress and is possibly involved in the regulation of FtsZ levels. Optimal intracellular levels of the essential cell-division protein FtsZ are critical for cell division and viability, overview
-
physiological function
-
FtsH is necessary for the processing of colicinsDand E3 during their import
-
physiological function
-
FtsH is a highly dynamic protease undergoing sequential transitions between five conformational states on the second timescale. Addition of ATP does not influence the number of states or change the timescale of domain motions but affects the state occupancy distribution leading to an interdomain compaction
-
physiological function
-
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA. MIT 9313 has less of the FtsH protease
-
physiological function
-
filamentation temperature-sensitive H, FtsH, is a membrane-anchored ATP-dependent metalloprotease
-
physiological function
-
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA
-
physiological function
-
deletion mutants of isoform FtsH1 display a severe growth retardation both in LB and M63 medium. The lag phase is extended from 6 to 8 h and retardation of growth at the second phase of the biphasic growth curve leads to a 1.5 h longer doubling time in the FtsH1 FtsH2 double mutant compared to the FtsH1 mutant. The FtsH2 mutant does not show a pronounced growth retardation phenotype. Deletion of FtsH1, but not FtsH2 moderately enhances sensitivity to a lethal heat shock. Deletion of FtsH1 causes a 13% reduction in swimming motility, which is 38% reduction the FtsH1 FtsH2 double deletion background. The FtsH1 mutant forms an undifferentiated flat biofilm. The FtsH1 FtsH2 double mutant forms dense irregular biofilm structures anchored to the substratum at a few contact points
-
physiological function
-
enzyme isoforms FtsH1 and FtsH2 contribute to motility and biofilm development, regulate pyoverdine and Pseudomonas quinolone signal production, and contribute to HOCl oxidative stress tolerance and aminoglycoside tolerance in planktonic culture and in biofilms of Pseudomonas aeruginosa. Isoform FtsH1 regulates autolysis
-
physiological function
Chlamydomonas reinhardtii cc5325
-
the enzyme is involved in the degradation of photodamaged D1 during the photosystem II repair cycle
-
additional information
-
ftsH interferes with the expression or activity of phosphatases RapA, RapB, RapE and Spo0E, and interferes with the phosphorylation status of Spo0A through Spo0E
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FTSH_AQUAE
Aquifex aeolicus (strain VF5)
634
0
70686
Swiss-Prot
other Location (Reliability: 4)
FTSH2_ARATH
695
0
74157
Swiss-Prot
other Location (Reliability: 1)
FTSH3_SYNY3
Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
616
0
67250
Swiss-Prot
other Location (Reliability: 2)
FTSH1_SYNY3
Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
665
0
72110
Swiss-Prot
-
FTSH4_SYNY3
Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
628
0
68199
Swiss-Prot
other Location (Reliability: 4)
FTSH6_ARATH
688
0
74515
Swiss-Prot
Secretory Pathway (Reliability: 2)
FTSH2_SYNY3
Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
627
0
68496
Swiss-Prot
-
Q7V8H0_PROMM
Prochlorococcus marinus (strain MIT 9313)
625
0
67490
TrEMBL
Secretory Pathway (Reliability: 1)
FTSHB_ARATH
806
0
88717
Swiss-Prot
other Location (Reliability: 1)
FTSH5_ARATH
704
0
75232
Swiss-Prot
Secretory Pathway (Reliability: 2)
FTSH9_ARATH
806
0
87838
Swiss-Prot
Secretory Pathway (Reliability: 5)
FTSH_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
610
0
68099
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115105
x * 115105, FtsH12, sequence calculation
66000
67250
-
x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
68199
-
x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
68496
-
x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
69304
-
x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
70000
73198
x * 73198, FtsH8, sequence calculation
74515
x * 74515, FtsH6, sequence calculation
75232
x * 75232, FtsH5, sequence calculation
76759
x * 76759, FtsH1, sequence calculation
77275
x * 77275, FtsH4, sequence calculation
78000
87802
x * 87802, FtsH7, sequence calculation
87838
x * 87838, FtsH9, sequence calculation
88717
x * 88717, FtsH11, sequence calculation
89353
x * 89353, FtsH3, sequence calculation
89555
x * 89555, FtsH10, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterohexamer
hexamer
homohexamer
additional information
?
x * 76759, FtsH1, sequence calculation
?
x * 89353, FtsH3, sequence calculation
?
x * 77275, FtsH4, sequence calculation
?
x * 75232, FtsH5, sequence calculation
?
x * 74515, FtsH6, sequence calculation
?
x * 87802, FtsH7, sequence calculation
?
x * 73198, FtsH8, sequence calculation
?
x * 87838, FtsH9, sequence calculation
?
x * 89555, FtsH10, sequence calculation
?
x * 88717, FtsH11, sequence calculation
?
x * 115105, FtsH12, sequence calculation
?
-
x * 68199, sll1463, sequence calculation, x * 68496, slr0228, sequence calculation, x * 67250, slr1640, sequence calculation, x * 69304, slr1390, sequence calculation
heterohexamer
-
the Arabidopsis thylakoid FtsH protease complex is composed of FtsH1/FtsH5 (type A) and FtsH2/FtsH8 (type B) subunits
heterohexamer
-
FtsH hexamer is composed of two A-type (FtsH 1 and 5) and four B-type (FtsH 2 and 8) subunits. FtsH monomers form an active hexamer in the thylakoid under light stress
heterohexamer
the thylakoid FtsH hexamer is composed of two type A (FtsH1) and four type B (FtsH8) subunits
heterohexamer
the thylakoid FtsH hexamer is composed of four type B (FtsH2 and FtsH8) subunits
heterohexamer
the thylakoid FtsH hexamer is composed of two type A (FtsH1 and FtsH5) subunits
heterohexamer
-
FtsH hexamer is composed of two A-type (FtsH 1 and 5) and four B-type (FtsH 2 and 8) subunits. FtsH monomers form an active hexamer in the thylakoid under light stress
heterohexamer
-
FtsH hexamer is composed of two A-type (FtsH 1 and 5) and four B-type (FtsH 2 and 8) subunits. FtsH monomers form an active hexamer in the thylakoid under light stress
hexamer
hexameric assembly consisting of a 6fold symmetric protease disk and a 2fold symmetric AAA ring
homohexamer
-
FtsH forms homohexameric ring structures and large heterocomplexes with HflK/C
homohexamer
-
6 * 66000, isoform FtsH1, calculated from amino acid sequence
additional information
-
ATP binding is not necessary for enzyme assembly, enzyme probably forms high molecular weight complexes
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
-
the duplicated genes, FTSH1 and FTSH5 (subunit type A) and FTSH2 and FTSH8 (subunit type B), are redundant.The presence of two types of subunits is essential for complex formation, photosystem II repair, and chloroplast biogenesis
additional information
-
interchangeability of subunits in chloroplast oligomeric complexes
additional information
-
FtsH2 and FtsH5 are present in a heteromeric complex
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes, but some might be homocomplexes composed of VAR2
additional information
-
the C-terminus comprise the cytoplasmic ATPase and protease domain. The ATPase domain contains the Walker A/B motifs and the second region of homology responsible for the binding and hydrolysis of ATP
additional information
comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases, modelling of the apo- and ADP bound state
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
FtsH is subject to selfprocessing and removes its C-terminal 7 amino acid residues
ubiquitylation
-
ubiquitylation of FtsH1 by AtCHIP might lead to the degradation of FtsH1 in vivo
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of a transmembrane helix-lacking FtsH construct from Aquifex aeolicus, at 2.9 A and 3.3 A resolution in space groups R32 and P312, respectively. In both structures, the FtsH hexamer is created from two different subunits of the asymmetric unit by the threefold symmetry of the crystals. All subunits are loaded with ADP. Within the ATPase cycle while the whole subunit switches from the opened to the closed state, pore loop-1 interacts with the substrate and translocates it into the proteolytic chamber
vapor diffusion method, using either 2 M ammonium sulfate, 0.1 M Tris-HCl pH 8.5, 10 mM EDTA or, as another condition, 60% tacsimate pH 7.0, 10 mM adenylyl imidodiphosphate lithium salt hydrate
cytosolic region of apo-FtsH, microbatch method by mixing equal volumes of 20 mg/ml protein with crystallization buffer containing 30% w/v PEG 400, 200 mM CaCl2, 100 mM HEPES, pH 7.5, 200 mM glycine, and 0.1-0.2% w/v low-melt agarose, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H417L
-
the mutant accumulates about 20% relative to the wild type enzyme and does not cleave delta32 protein
H488L
-
the FtsH2 mutation inhibits zinc binding and inactivates proteolysis
E439Q
-
inactive, the mutation abolishes the binding of the catalytic zinc ion
A359V
homolog of the human pathogenic A510V mutation of paraplegin (SPG7), does not affect the dynamic behavior of the protease but impairs the ATP-coupled domain compaction
G404L
site-directed mutagenesis, the mutant is monomeric and inactive in the ATPase assay and possesses only very low proteolytic activity
A359V
-
homolog of the human pathogenic A510V mutation of paraplegin (SPG7), does not affect the dynamic behavior of the protease but impairs the ATP-coupled domain compaction
-
additional information
additional information
-
a FtsH11 null mutant (salk033047) displays thermosensitive phenotypes using both acquired and basal thermotolerance assays
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH8 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V
additional information
-
ectopic expression of cGPA1 rescues the leaf variegation of ftsh2 and partially corrects mis-regulated gene expression in thf1, the leaf-variegated mutant thylakoid formation 1, phenotype, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the cells in green sectors of variegation mutant var2 have normal-appearing chloroplasts whereas cells in the white sectors have abnormal plastids that lack pigments and organized lamellae. The mutant serves as threshold model in which the formation of chloroplasts is due to the presence of activities/processes that are able to compensate for a lack of VAR2, mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation, phenotype and mutant screening, detailed overview. The enhancement in green sector formation is accompanied by an increased accumulation of chloroplast FtsH mRNA and protein. Overexpressionj of isozyme AtFtsH8 suppresses the var2 phenotype. Isolation and analysis of mutant svr1-1, i.e. suppression of variegation1-1, and of svr2 mutant, overview. Examples of var2 suppressors are clpC2, fug1, sco1, and GPA1, mutational effets, overview
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH1 shows no visible phenotype
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II
additional information
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generation of ftsH knockouts, that show a sporulation frequency reduced by several orders of magnitude. The combination of ftsH knockout with knockout of one of the phosphatases RapA, RapB, RapE or Spo0E results in a sporulation frequency, that is increased by two to three orders of magnitude, but still remains below 1% of wild-type level, overview
additional information
-
mutants lacking 5 or 10 amino acid residues in the exposed N-terminal region of the D1 protein are blocked in the synthesis of D1 protein, photosystem II repair and selective D1 degradation are inhibited in the A20 truncation mutant
additional information
-
insertional inactivation of two of the four genes, slr1390 and slr1604, is lethal, while inactivation of sll1463 does not have an obvious affect and inactivation of slr0228 produces cells with altered pigmentation and a significant reduction in the amount of PSI
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
under light stress conditions (intensity, 1 mM of photons m-2 s-1), FtsH hexamers in thylakoids are stable even in longer stress periods
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione agarose column chromatography and Ni-NTA column chromatography
-
Ni-NTA column chromatography, Resource Q anion-exchange chromatography, and Superdex 16/6000 gel filtration
partially
recombinant amino acids 147-610 of FtsH with K410L-K415A surface mutations, and recombinant G404L and K207A mutants
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
4 alleles of gene var2, positional cloning, initiation of chromosome walking of the var2 gene on chromosome 2, amino acid sequence determination, mechanism of genetic variation
DNA and amino acid sequence determination and analysis, in vitro translation and import into isolated Pisum sativum chloroplasts, where the enzyme is processed to its mature form and targeted into the thylakoid membrane
expressed in Escherichia coli BL21(DE3) cells
expression of amino acids 147-610 of FtsH with K410L-K415A surface mutations, and expression of G404L and K207A mutants
expression of GST-tagged wild-type and mutant enzymes in Escherichia coli ftsh-deficient strain A8296
-
genes ftsH-1, ftsH-2, ftsH-3, and ftsH-4, DNA and amino acid sequence determination and analysis, quantitative real time RT-PCR expression anaylsis
-
genetic allelic variants of gene var2, i.e. AtFtsH2, DNA and amino acid sequence determination and analysis
ZmFtsH2A, DNA and amino acid sequence determination and analysis, expression of ZmFtsH2A in Nicotiana tabacum transgenic plants using the Agrobacterium tumefaciens strain LBA4404 freeze-thaw transfection method. The full length gene is cloned into a binary vector pCAMBIA1300-35SMCSnos-als containing a constitutive CaMV35S promoter, a nos terminiter, and a mutational chlorsulfuron-resistance acetolactate synthase gene from Arabidopsis thaliana
ZmFtsH2B, DNA and amino acid sequence determination and analysis, expression of ZmFtsH2B in Nicotiana tabacum transgenic plants using the Agrobacterium tumefaciens strain LBA4404 freeze-thaw transfection method. The full length gene is cloned into a binary vector pCAMBIA1300-35SMCSnos-als containing a constitutive CaMV35S promoter, a nos terminiter, and a mutational chlorsulfuron-resistance acetolactate synthase gene from Arabidopsis thaliana
DNA and amino acid sequence determination and analysis, in vitro translation and import into isolated Pisum sativum chloroplasts, where the enzyme is processed to its mature form and targeted into the thylakoid membrane
DNA and amino acid sequence determination and analysis, in vitro translation and import into isolated Pisum sativum chloroplasts, where the enzyme is processed to its mature form and targeted into the thylakoid membrane
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
construction of a DELTAPsbO/DELTASlr0228 double mutant strain that shows the presence of newly synthesized, unassembled D1 protein, especially its non-mature forms pD1 and iD1, not observed in the not in the DELTAPsbO single mutant. Inactivation of the slr0228 gene in the DELTAPsbV strain markedly increases the accumulation the monomeric PSII core complex RCC(1) and RC47 complex, the core complex lacking the inner antenna CP43, but still there is no accumulation of the dimeric PSII core complex RCC(2)
ethyl methanesulfonate can cause loss-of-function mutations in gene var2, D1 degradation is impaired in var2 mutant
ftsH expression levels are upregulated upon exposure to agents that produce reactive oxygen and nitrogen intermediates and growth in macrophages
mRNA levels of isoforms Ftsh1 and Ftsh increase upon high light exposure
A8IL08; A8J6C7
the knockout mutant of gene AtFtsH11 shows a phenotype susceptible to high temperature stress
ftsH expression levels are upregulated upon exposure to agents that produce reactive oxygen and nitrogen intermediates and growth in macrophages
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ftsH expression levels are upregulated upon exposure to agents that produce reactive oxygen and nitrogen intermediates and growth in macrophages
-
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REF.
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts
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Spinacia oleracea
brenda
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56
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2005
Synechocystis sp.
brenda
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Quality control of Photosystem II: an FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions
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4
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2005
Synechocystis sp.
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Two types of FtsH protease subunits are required for chloroplast biogenesis and photosystem II repair in Arabidopsis
Plant Cell
17
2782-2790
2005
Arabidopsis thaliana (Q39102), Arabidopsis thaliana (O80860), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana
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The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes
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Arabidopsis thaliana
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48
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Arabidopsis thaliana
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Proc. Natl. Acad. Sci. USA
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brenda
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The significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes
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-
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-
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brenda
Bandyopadhyay, K.; Parua, P.K.; Datta, A.B.; Parrack, P.
Escherichia coli HflK and HflC can individually inhibit the HflB (FtsH)-mediated proteolysis of lambdaCII in vitro
Arch. Biochem. Biophys.
501
239-243
2010
Escherichia coli
brenda
Komenda, J.; Knoppova, J.; Krynicka, V.; Nixon, P.J.; Tichy, M.
Role of FtsH2 in the repair of photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assembly or stability of the CaMn4 cluster
Biochim. Biophys. Acta
1797
566-575
2010
Synechocystis sp. (Q55700), Synechocystis sp.
brenda
Liu, X.; Yu, F.; Rodermel, S.
Arabidopsis chloroplast FtsH, var2 and suppressors of var2 leaf variegation: a review
J. Integr. Plant Biol.
52
750-761
2010
Arabidopsis thaliana (Q39102), Arabidopsis thaliana (O80860), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q9SD67), Escherichia coli, Synechocystis sp.
brenda
Ayuso-Tejedor, S.; Nishikori, S.; Okuno, T.; Ogura, T.; Sancho, J.
FtsH cleavage of non-native conformations of proteins
J. Struct. Biol.
171
117-124
2010
Escherichia coli
brenda
Le, A.T.; Schumann, W.
The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease
Microbiology
155
1122-1132
2009
Bacillus subtilis
brenda
Yue, G.; Hu, X.; He, Y.; Yang, A.; Zhang, J.
Identification and characterization of two members of the FtsH gene family in maize (Zea mays L.)
Mol. Biol. Rep.
37
855-863
2010
Zea mays (B1P2H3), Zea mays (B1P2H4), Zea mays, Zea mays DH4866 (B1P2H3), Zea mays DH4866 (B1P2H4)
brenda
Yamamoto, Y.; Aminaka, R.; Yoshioka, M.; Khatoon, M.; Komayama, K.; Takenaka, D.; Yamashita, A.; Nijo, N.; Inagawa, K.; Morita, N.; Sasaki, T.; Yamamoto, Y.
Quality control of photosystem II: impact of light and heat stresses
Photosynth. Res.
98
589-608
2008
Spinacia oleracea, Synechocystis sp., Escherichia coli (P0AAI3), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (O80860), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q9SD67)
-
brenda
Zhang, L.; Wei, Q.; Wu, W.; Cheng, Y.; Hu, G.; Hu, F.; Sun, Y.; Zhu, Y.; Sakamoto, W.; Huang, J.
Activation of the heterotrimeric G protein alpha-subunit GPA1 suppresses the ftsh-mediated inhibition of chloroplast development in Arabidopsis
Plant J.
58
1041-1053
2009
Arabidopsis thaliana
brenda
Bieniossek, C.; Niederhauser, B.; Baumann, U.M.
The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation
Proc. Natl. Acad. Sci. USA
106
21579-21584
2009
Thermotoga maritima (Q9WZ49)
brenda
Gomez-Baena, G.; Rangel, O.A.; Lopez-Lozano, A.; Garcia-Fernandez, J.M.; Diez, J.
Stress responses in Prochlorococcus MIT9313 vs. SS120 involve differential expression of genes encoding proteases ClpP, FtsH and Lon
Res. Microbiol.
160
567-575
2009
Prochlorococcus marinus
brenda
Narberhaus, F.; Obrist, M.; Fuehrer, F.; Langklotz, S.
Degradation of cytoplasmic substrates by FtsH, a membrane-anchored protease with many talents
Res. Microbiol.
160
652-659
2009
Escherichia coli
brenda
Kiran, M.; Chauhan, A.; Dziedzic, R.; Maloney, E.; Mukherji, S.K.; Madiraju, M.; Rajagopalan, M.
Mycobacterium tuberculosis ftsH expression in response to stress and viability
Tuberculosis
89 Suppl 1
S70-S73
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Yoshioka, M.; Nakayama, Y.; Yoshida, M.; Ohashi, K.; Morita, N.; Kobayashi, H.; Yamamoto, Y.
Quality control of photosystem II: FtsH hexamers are localized near photosystem II at grana for the swift repair of damage
J. Biol. Chem.
285
41972-41981
2010
Spinacia oleracea
brenda
Chauleau, M.; Mora, L.; Serba, J.; de Zamaroczy, M.
FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm
J. Biol. Chem.
286
29397-29407
2011
Escherichia coli
brenda
Yoshioka, M.; Yamamoto, Y.
Quality control of Photosystem II: Where and how does the degradation of the D1 protein by FtsH proteases start under light stress? - Facts and hypotheses
J. Photochem. Photobiol. B
104
229-235
2011
Synechocystis sp., Arabidopsis thaliana, Spinacia oleracea
brenda
Kato, Y.; Kouso, T.; Sakamoto, W.
Variegated tobacco leaves generated by chloroplast FtsH suppression: implication of FtsH function in the maintenance of thylakoid membranes
Plant Cell Physiol.
53
391-404
2012
Nicotiana tabacum
brenda
Zhang, D.; Kato, Y.; Zhang, L.; Fujimoto, M.; Tsutsumi, N.; Sodmergen, N.; Sakamoto, W.
The FtsH protease heterocomplex in Arabidopsis: dispensability of type-B protease activity for proper chloroplast development
Plant Cell
22
3710-3725
2010
Arabidopsis thaliana
brenda
Adam, Z.; Frottin, F.; Espagne, C.; Meinnel, T.; Giglione, C.
Interplay between N-terminal methionine excision and FtsH protease is essential for normal chloroplast development and function in Arabidopsis
Plant Cell
23
3745-3760
2011
Arabidopsis thaliana
brenda
Rodrigues, R.A.; Silva-Filho, M.C.; Cline, K.
FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex
Plant J.
65
600-609
2011
Arabidopsis thaliana
brenda
Vostrukhina, M.; Popov, A.; Brunstein, E.; Lanz, M.A.; Baumgartner, R.; Bieniossek, C.; Schacherl, M.; Baumann, U.
The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C2-symmetric hexamer
Acta Crystallogr. Sect. D
71
1307-1318
2015
Aquifex aeolicus (O67077)
brenda
Yoshioka-Nishimura, M.; Yamamoto, Y.
Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes
J. Photochem. Photobiol. B
137
100-106
2014
Arabidopsis thaliana, Spinacia oleracea
-
brenda
Krynicka, V.; Tichy, M.; Krafl, J.; Yu, J.; Ka?a, R.; Boehm, M.; Nixon, P.J.; Komenda, J.
Two essential FtsH proteases control the level of the Fur repressor during iron deficiency in the cyanobacterium Synechocystis sp. PCC 6803
Mol. Microbiol.
94
609-624
2014
Synechocystis sp. (Q55700), Synechocystis sp. (P73437), Synechocystis sp. (P72991), Synechocystis sp. (P73179), Synechocystis sp.
brenda
Sacharz, J.; Bryan, S.J.; Yu, J.; Burroughs, N.J.; Spence, E.M.; Nixon, P.J.; Mullineaux, C.W.
Sub-cellular location of FtsH proteases in the cyanobacterium Synechocystis sp. PCC 6803 suggests localised PSII repair zones in the thylakoid membranes
Mol. Microbiol.
96
448-462
2015
Synechocystis sp. (Q55700), Synechocystis sp. (P73437), Synechocystis sp. (P72991), Synechocystis sp. (P73179), Synechocystis sp.
brenda
Seemueller, E.; Sule, S.; Kube, M.; Jelkmann, W.; Schneider, B.
The AAA+ ATPases and HflB/FtsH proteases of Candidatus Phytoplasma mali: phylogenetic diversity, membrane topology, and relationship to strain virulence
Mol. Plant Microbe Interact.
26
367-376
2013
Candidatus Phytoplasma mali
brenda
Campbell, D.A.; Hossain, Z.; Cockshutt, A.M.; Zhaxybayeva, O.; Wu, H.; Li, G.
Photosystem II protein clearance and FtsH function in the diatom Thalassiosira pseudonana
Photosynth. Res.
115
43-54
2013
Thalassiosira pseudonana
brenda
Wagner, R.; Aigner, H.; Funk, C.
FtsH proteases located in the plant chloroplast
Physiol. Plant.
145
203-214
2012
Arabidopsis thaliana
brenda
Yoshioka-Nishimura, M.; Nanba, D.; Takaki, T.; Ohba, C.; Tsumura, N.; Morita, N.; Sakamoto, H.; Murata, K.; Yamamoto, Y.
Quality control of photosystem II: direct imaging of the changes in the thylakoid structure and distribution of FtsH proteases in spinach chloroplasts under light stress
Plant Cell Physiol.
55
1255-1265
2014
Spinacia oleracea
brenda
Boehm, M.; Yu, J.; Krynicka, V.; Barker, M.; Tichy, M.; Komenda, J.; Nixon, P.J.; Nield, J.
Subunit organization of a Synechocystis hetero-oligomeric thylakoid FtsH complex involved in photosystem II repair
Plant Cell
24
3669-3683
2012
Synechocystis sp. (Q55700), Synechocystis sp.
brenda
Malnoe, A.; Wang, F.; Girard-Bascou, J.; Wollman, F.A.; de Vitry, C.
Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas reinhardtii under stress conditions
Plant Cell
26
373-390
2014
Chlamydomonas reinhardtii (A8IL08), Chlamydomonas reinhardtii
brenda
Zhang, S.; Zhang, D.; Yang, C.
AtFtsH4 perturbs the mitochondrial respiratory chain complexes and auxin homeostasis in Arabidopsis
Plant Signal. Behav.
9
1-4
2014
Arabidopsis thaliana
brenda
Moldavski, O.; Levin-Kravets, O.; Ziv, T.; Adam, Z.; Prag, G.
The hetero-hexameric nature of a chloroplast AAA+ FtsH protease contributes to its thermodynamic stability
PLoS ONE
7
e36008
2012
Arabidopsis thaliana, Arabidopsis thaliana (O80860), Arabidopsis thaliana (Q9FH02)
brenda
Tanveer, A.; Allen, S.M.; Jackson, K.E.; Charan, M.; Ralph, S.A.; Habib, S.
An FtsH protease is recruited to the mitochondrion of Plasmodium falciparum
PLoS ONE
8
e74408
2013
Plasmodium falciparum
brenda
Chen, J.; Burke, J.J.; Xin, Z.
Chlorophyll fluorescence analysis revealed essential roles of FtsH11 protease in regulation of the adaptive responses of photosynthetic systems to high temperature
BMC Plant Biol.
18
11
2018
Arabidopsis thaliana (Q9FGM0)
brenda
Kamal, S.; Rybtke, M.; Nimtz, M.; Sperlein, S.; Giske, C.; Trcek, J.; Deschamps, J.; Briandet, R.; Dini, L.; Jaensch, L.; Tolker-Nielsen, T.; Lee, C.; Roemling, U.
Two FtsH proteases contribute to fitness and adaptation of Pseudomonas aeruginosa clone C strains
Front. Microbiol.
10
1372
2019
Pseudomonas aeruginosa, Pseudomonas aeruginosa SG17M
brenda
Adam, Z.; Aviv-Sharon, E.; Keren-Paz, A.; Naveh, L.; Rozenberg, M.; Savidor, A.; Chen, J.
The chloroplast envelope protease FTSH11 - interaction with CPN60 and identification of potential substrates
Front. Plant Sci.
10
428
2019
Arabidopsis thaliana, Arabidopsis thaliana (Q9FGM0)
brenda
Ruer, M.; Krainer, G.; Groeger, P.; Schlierf, M.
ATPase and protease domain movements in the bacterial AAA+ protease FtsH are driven by thermal fluctuations
J. Mol. Biol.
430
4592-4602
2018
Thermotoga maritima (Q9WZ49), Thermotoga maritima DSM 3109 (Q9WZ49)
brenda
Uthoff, M.; Baumann, U.
Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+ protease FtsH
J. Struct. Biol.
204
199-206
2018
Aquifex aeolicus (O67077)
brenda
Wang, F.; Qi, Y.; Malnoe, A.; Choquet, Y.; Wollman, F.A.; de Vitry, C.
The high light response and redox control of thylakoid FtsH protease in Chlamydomonas reinhardtii
Mol. Plant
10
99-114
2017
Chlamydomonas reinhardtii (A8IL08 and A8J6C7), Chlamydomonas reinhardtii
brenda
Krynicka, V.; Shao, S.; Nixon, P.J.; Komenda, J.
Accessibility controls selective degradation of photosystem II subunits by FtsH protease
Nat. Plants
1
15168
2015
Synechocystis sp. PCC 6803 (Q55700 and P72991)
brenda
Beckova, M.; Yu, J.; Krynicka, V.; Kozlo, A.; Shao, S.; Konik, P.; Komenda, J.; Murray, J.W.; Nixon, P.J.
Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria
Philos. Trans. R. Soc. Lond. B Biol. Sci.
372
20160394
2017
Synechocystis sp. PCC 6803 (Q55700 and P72991)
brenda
Shao, S.; Cardona, T.; Nixon, P.
Early emergence of the FtsH proteases involved in photosystem II repair
Photosynthetica
56
163-177
2018
cellular organisms
-
brenda
Bonisteel, E.; Turner, B.; Murphy, C.; Melanson, J.; Duff, N.; Beardsall, B.; Xu, K.; Campbell, D.; Cockshutt, A.
Strain specific differences in rates of photosystem II repair in picocyanobacteria correlate to differences in FtsH protein levels and isoform expression patterns
PLoS ONE
13
e0209115
2018
Prochlorococcus marinus (Q7V8H0), Prochlorococcus marinus, Prochlorococcus marinus subsp. pastoris (Q7V1V9 and Q7V362), Prochlorococcus marinus MIT 9313 (Q7V8H0), Prochlorococcus marinus subsp. pastoris MED4 (Q7V1V9 and Q7V362)
brenda
Wang, L.; Kim, C.; Xu, X.; Piskurewicz, U.; Dogra, V.; Singh, S.; Mahler, H.; Apel, K.
Singlet oxygen- and EXECUTER1-mediated signaling is initiated in grana margins and depends on the protease FtsH2
Proc. Natl. Acad. Sci. USA
113
E3792-E3800
2016
Arabidopsis thaliana (O80860)
brenda
Konik, P.; Skotnicova, P.; Gupta, S.; Tichy, M.; Sharma, S.; Komenda, J.; Sobotka, R.; Krynicka, V.
The cyanobacterial FtsH4 protease controls accumulation of protein factors involved in the biogenesis of photosystem I
Biochim. Biophys. Acta Bioenerg.
1865
149017
2024
Synechocystis sp. PCC 6803
brenda
Liu, W.; Schoonen, M.; Wang, T.; McSweeney, S.; Liu, Q.
Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state
Commun. Biol.
5
257
2022
Thermotoga maritima (Q9WZ49)
brenda
Kato, Y.; Kuroda, H.; Ozawa, S.I.; Saito, K.; Dogra, V.; Scholz, M.; Zhang, G.; de Vitry, C.; Ishikita, H.; Kim, C.; Hippler, M.; Takahashi, Y.; Sakamoto, W.
Characterization of tryptophan oxidation affecting D1 degradation by FtsH in the photosystem II quality control of chloroplasts
eLife
12
RP88822
2023
Arabidopsis thaliana
brenda
Yi, L.; Liu, B.; Nixon, P.J.; Yu, J.; Chen, F.
Recent advances in understanding the structural and functional evolution of FtsH proteases
Front. Plant Sci.
13
837528
2022
Synechocystis sp. PCC 6803
brenda
Mishra, L.S.; Funk, C.
The FtsHi enzymes of Arabidopsis thaliana pseudo-proteases with an important function
Int. J. Mol. Sci.
22
5917
2021
Arabidopsis thaliana
brenda
Yeo, W.S.; Anokwute, C.; Marcadis, P.; Levitan, M.; Ahmed, M.; Bae, Y.; Kim, K.; Kostrominova, T.; Liu, Q.; Bae, T.
A membrane-bound transcription factor is proteolytically regulated by the AAA+ protease FtsH in Staphylococcus aureus
J. Bacteriol.
202
e00019-20
2020
Staphylococcus aureus
brenda
Mielke, K.; Wagner, R.; Mishra, L.S.; Demir, F.; Perrar, A.; Huesgen, P.F.; Funk, C.
Abundance of metalloprotease FtsH12 modulates chloroplast development in Arabidopsis thaliana
J. Exp. Bot.
72
3455-3473
2021
Arabidopsis thaliana
brenda
Fu, W.; Cui, Z.; Guo, J.; Cui, X.; Han, G.; Zhu, Y.; Hu, J.; Gao, X.; Li, Y.; Xu, M.; Fu, A.; Wang, F.
Immunophilin CYN28 is required for accumulation of photosystem II and thylakoid FtsH protease in Chlamydomonas
Plant Physiol.
191
1002-1016
2023
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii cc5325
brenda
Lei, Y.; Li, B.; Wang, X.; Wei, J.; Wang, P.; Zhao, J.; Yu, F.; Qi, Y.
Chloroplast SRP54 and FtsH protease coordinate thylakoid membrane-associated proteostasis in Arabidopsis
Plant Physiol.
192
2318-2335
2023
Arabidopsis thaliana
brenda
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