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damaged PSII D1 protein + H2O
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 -
-
-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
D1 protein + H2O
?
-
-
-
-
?
damaged PSII D1 protein + H2O
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 -
-
-
?
delta32 protein + H2O
?
-
-
-
-
?
EX1 + H2O
?
substrate chloroplast protein EXECUTER1, involved in signaling by singlet oxygen
-
-
?
heat shock transcription factor sigma 32 + H2O
?
-
-
-
-
?
light-harvesting complex II + H2O
?
-
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
-
-
?
photodamaged D1 protein + H2O
?
photodamaged D2 protein + H2O
?
-
-
-
-
?
protein lambdaCII + H2O
?
-
-
-
-
?
protein sigma32 + H2O
?
-
-
-
-
?
proteins + H2O
peptides
-
-
?
Rieske FeS protein + H2O
?
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
additional information
?
-
23 kDa fragment of photosystem II D1 protein + H2O
?
-
-
-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
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
-
?
photodamaged D1 protein + H2O
?
-
-
-
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
Protein + H2O
?
-
FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II from photoinhibition, and the formation of thylakoids
-
-
?
Protein + H2O
?
-
FtsH11 protease plays a critical role in Arabidopsis thermotolerance. FtsH11 constitutively protects the photosynthesis apparatus from the damage caused by elevated temperatures
-
-
?
Protein + H2O
?
-
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
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein + H2O
peptides
-
unfoldase activity might be a common property of ATP-dependent proteases
-
?
protein + H2O
peptides
degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein + H2O
peptides
enzyme is involved in chloroplast biogenesis
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
-
the D1 protein, a core subunit of the PSII reaction enter, is a substrate for FtsH protease
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
damaged PSII D1 protein + H2O
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 -
-
-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
-
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
-
?
D1 protein + H2O
?
-
-
-
-
?
damaged PSII D1 protein + H2O
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 -
-
-
?
delta32 protein + H2O
?
-
-
-
-
?
heat shock transcription factor sigma 32 + H2O
?
-
-
-
-
?
light-harvesting complex II + H2O
?
-
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
-
-
?
photodamaged D1 protein + H2O
?
photodamaged D2 protein + H2O
?
-
-
-
-
?
proteins + H2O
peptides
-
-
?
Rieske FeS protein + H2O
?
-
degradation of membrane protein, essentially required as a membrane-integrated quality control
-
?
additional information
?
-
photodamaged D1 protein + H2O
?
-
-
-
-
?
photodamaged D1 protein + H2O
?
-
-
the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
-
?
Protein + H2O
?
-
FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II from photoinhibition, and the formation of thylakoids
-
-
?
Protein + H2O
?
-
FtsH11 protease plays a critical role in Arabidopsis thermotolerance. FtsH11 constitutively protects the photosynthesis apparatus from the damage caused by elevated temperatures
-
-
?
Protein + H2O
?
-
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
-
-
?
protein + H2O
peptides
-
degradation of membrane proteins, essentially required as a membrane-integrated quality control
-
?
protein + H2O
peptides
degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
-
?
protein + H2O
peptides
enzyme is involved in chloroplast biogenesis
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
-
-
?
additional information
?
-
-
the D1 protein, a core subunit of the PSII reaction enter, is a substrate for FtsH protease
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 FtsH gene multiplication is of adaptive value during the course of evolution of oxygenic photosynthesis
metabolism
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 enzyme regulation, overview
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 the ATP-dependent zinc metallopeptidase is a cell division protein
evolution
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 FtsH gene multiplication is of adaptive value during the course of evolution of oxygenic photosynthesis
malfunction
-
mutants lacking isoforms FtsH2 and FtsH5 are characterized by a typical leaf-variegated phenotype
malfunction
-
the loss of isoform FtsH4 regulates Arabidopsis development and architecture by mediating the peroxidase-dependent interplay between hydrogen peroxide and auxin homeostasis
metabolism
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 enzyme regulation, overview
metabolism
-
FtsH5/VAR1, FtsH2/VAR2, VAR3 and THF1 control leaf variegation in Arabidopsis thaliana
metabolism
-
the thylakoid located FtsH complex in Arabidopsis is responsible for degradation of photodamaged D1 protein in concert with lumenal Deg proteases
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
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 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
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 the ATP-dependent zinc metallopeptidase is a cell division protein
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 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
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 the ATP-dependent zinc metallopeptidase is involved in the degradation of both Lhcb3 and Lhcb1 during senescence and high-light acclimation
physiological function
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 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
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 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
-
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
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 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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 89353, FtsH3, sequence calculation
?
x * 78000, SDS-PAGE
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 115105, FtsH12, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 73198, FtsH8, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 74515, FtsH6, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 75232, FtsH5, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 76759, FtsH1, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 77275, FtsH4, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 87802, FtsH7, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 87838, FtsH9, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 88717, FtsH11, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 89353, FtsH3, sequence calculation
?
O80860, O80983, Q1PDW5, Q39102, Q84WU8, Q8VZI8, Q8W585, Q9FGM0, Q9FH02, Q9FIM2, Q9SAJ3, Q9SD67 x * 89555, FtsH10, sequence calculation
heterohexamer
-
-
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 Arabidopsis thylakoid FtsH protease complex is composed of FtsH1/FtsH5 (type A) and FtsH2/FtsH8 (type B) 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
the thylakoid FtsH hexamer is composed of two type A (FtsH1) and four type B (FtsH8) subunits
additional information
-
ATP binding is not necessary for enzyme assembly, enzyme probably forms high molecular weight complexes
additional information
-
FtsH2 and FtsH5 are present in a heteromeric complex
additional information
-
interchangeability of subunits in chloroplast oligomeric 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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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D326N
-
the mutant does not cleave delta32 protein
G195D
-
the mutant does not cleave delta32 protein
G267D
-
the mutant does not cleave delta32 protein
G302S
-
the mutant does not cleave delta32 protein
G433R
-
the mutant does not cleave delta32 protein
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
P320L
-
the mutant does not cleave delta32 protein
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
-
construction of deficient mutant
additional information
-
a FtsH11 null mutant (salk033047) displays thermosensitive phenotypes using both acquired and basal thermotolerance assays
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 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 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
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
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 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
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Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Arabidopsis thaliana (O80860)
brenda
Langer, T.; Kaser, M.; Klanner, C.; Leonhard, K.
AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis
Biochem. Soc. Trans.
29
431-436
2001
Arabidopsis thaliana
brenda
Lindahl, M.; Tabak, S.; Cseke, L.; Pichersky, E.; Andersson, B.; Adam, Z.
Identification, characterization, and molecular cloning of a homologue of the bacterial FtsH protease in chloroplasts of higher plants
J. Biol. Chem.
271
29329-29334
1996
Arabidopsis thaliana (Q39102), Pisum sativum, Spinacia oleracea
brenda
Bailey, S.; Thompson, E.; Nixon, P.J.; Horton, P.; Mullineaux, C.W.; Robinson, C.; Mann, N.H.
A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo
J. Biol. Chem.
277
2006-2011
2002
Arabidopsis thaliana
brenda
Chen, M.; Choi, Y.; Voytas, D.F.; Rodermel, S.
Mutations in the Arabidopsis VAR2 locus cause leaf variegation due to the loss of a chloroplast FtsH protease
Plant J.
22
303-313
2000
Arabidopsis thaliana (Q39102)
brenda
Adam, Z.
The chloroplast proteolytic machinery
Annu. Plant Rev.
13
214-236
2005
Synechocystis sp., Arabidopsis thaliana
-
brenda
Adam, Z.; Rudella, A.; van Wijk, K.J.
Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts
Curr. Opin. Plant Biol.
9
234-240
2006
Arabidopsis thaliana
brenda
Zaltsman, A.; Ori, N.; Adam, Z.
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 (O80860), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana
brenda
Yu, F.; Park, S.; Rodermel, S.R.
The Arabidopsis FtsH metalloprotease gene family: interchangeability of subunits in chloroplast oligomeric complexes
Plant J.
37
864-876
2004
Arabidopsis thaliana
brenda
Zaltsman, A.; Feder, A.; Adam, Z.
Developmental and light effects on the accumulation of FtsH protease in Arabidopsis chloroplasts--implications for thylakoid formation and photosystem II maintenance
Plant J.
42
609-617
2005
Arabidopsis thaliana
brenda
Chen, J.; Burke, J.J.; Velten, J.; Xin, Z.
FtsH11 protease plays a critical role in Arabidopsis thermotolerance
Plant J.
48
73-84
2006
Arabidopsis thaliana
brenda
Sinvany-Villalobo, G.; Davydov, O.; Ben-Ari, G.; Zaltsman, A.; Raskind, A.; Adam, Z.
Expression in multigene families. Analysis of chloroplast and mitochondrial proteases
Plant Physiol.
135
1336-1345
2004
Arabidopsis thaliana
brenda
Yu, F.; Park, S.; Rodermel, S.R.
Functional redundancy of AtFtsH metalloproteases in thylakoid membrane complexes
Plant Physiol.
138
1957-1966
2005
Arabidopsis thaliana
brenda
Zelisko, A.; Garcia-Lorenzo, M.; Jackowski, G.; Jansson, S.; Funk, C.
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
Proc. Natl. Acad. Sci. USA
102
13699-13704
2005
Arabidopsis thaliana
brenda
Kolodziejczak, M.; Gibala, M.; Urantowka, A.; Janska, H.
The significance of Arabidopsis AAA proteases for activity and assembly/stability of mitochondrial OXPHOS complexes
Physiol. Plant.
129
135-142
2007
Arabidopsis thaliana
brenda
Shen, G.; Adam, Z.; Zhang, H.
The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts
Plant J.
52
309-321
2007
Arabidopsis thaliana
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 (O80860), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q9SD67), Escherichia coli, Synechocystis sp.
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
Arabidopsis thaliana (O80860), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q9SD67), Escherichia coli (P0AAI3), Spinacia oleracea, Synechocystis sp.
-
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
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
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
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
Wagner, R.; Aigner, H.; Funk, C.
FtsH proteases located in the plant chloroplast
Physiol. Plant.
145
203-214
2012
Arabidopsis thaliana
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
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
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 (Q9FGM0)
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