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Literature summary for 3.4.24.B20 extracted from

  • Liu, X.; Yu, F.; Rodermel, S.
    Arabidopsis chloroplast FtsH, var2 and suppressors of var2 leaf variegation: a review (2010), J. Integr. Plant Biol., 52, 750-761.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP dependent on Escherichia coli
ATP dependent on Synechocystis sp.
ATP dependent on Arabidopsis thaliana
ATP dependent on, Var2 contains an ATP-binding site, the second region of homology or SRH domain Arabidopsis thaliana

Cloned(Commentary)

Cloned (Comment) Organism
genetic allelic variants of gene var2, i.e. AtFtsH2, DNA and amino acid sequence determination and analysis Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
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 Synechocystis sp.
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 Arabidopsis thaliana
additional information the knockout mutant of gene AtFtsH1 shows no visible phenotype Arabidopsis thaliana
additional information the knockout mutant of gene AtFtsH10 shows reduced activity of mitochondrial complex I and V Arabidopsis thaliana
additional information the knockout mutant of gene AtFtsH3 shows reduced activity of mitochondrial complex I and V Arabidopsis thaliana
additional information the knockout mutant of gene AtFtsH4 shows altered late rosette leaf development and chloroplasts and mitochondria ultrastructure under short-day conditions Arabidopsis thaliana
additional information the knockout mutant of gene AtFtsH4 shows no visible phenotype, but is unable to degrade LHC II Arabidopsis thaliana
additional information the knockout mutant of gene AtFtsH5 shows variegated leaves, overexpression of isozyme AtFtsH1 suppresses the var1 phenotype Arabidopsis thaliana
additional information the knockout mutant of gene AtFtsH8 shows no visible phenotype Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Synechocystis sp. 9507
-
chloroplast
-
Arabidopsis thaliana 9507
-
mitochondrion
-
Arabidopsis thaliana 5739
-
additional information FtsH co-purifies with PSII complexes in Synechocystis Synechocystis sp.
-
-
plasma membrane
-
Escherichia coli 5886
-
thylakoid membrane
-
Synechocystis sp. 42651
-
thylakoid membrane
-
Arabidopsis thaliana 42651
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required Escherichia coli
Zn2+ required Synechocystis sp.
Zn2+ required Arabidopsis thaliana
Zn2+ required, Var2 contains a Zn-binding site, HEXXH, in their protease domain Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Arabidopsis thaliana the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence ?
-
?
additional information Escherichia coli 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana O80860 gene AtFtsH2 or var2; gene var2 variations, different mutated alleles, overview
-
Arabidopsis thaliana O80983 gene AtFtsH4; gene AtFtsH4
-
Arabidopsis thaliana Q1PDW5 gene AtFtsH6; gene AtFtsH6
-
Arabidopsis thaliana Q39102 gene AtFtsH1; gene AtFtsH1
-
Arabidopsis thaliana Q84WU8 gene AtFtsH3; gene AtFtsH3
-
Arabidopsis thaliana Q8VZI8 gene AtFtsH10; gene AtFtsH10
-
Arabidopsis thaliana Q8W585 gene AtFtsH8; gene AtFtsH8
-
Arabidopsis thaliana Q9FGM0 gene AtFtsH11; gene AtFtsH11
-
Arabidopsis thaliana Q9FH02 gene AtFtsH5 or var1; gene AtFtsH5 or var1
-
Arabidopsis thaliana Q9FIM2 gene AtFtsH9; gene AtFtsH9
-
Arabidopsis thaliana Q9SAJ3 gene AtFtsH12; gene AtFtsH12
-
Arabidopsis thaliana Q9SD67 gene AtFtsH7; gene AtFtsH7
-
Escherichia coli
-
-
-
Synechocystis sp.
-
four FtsH-like genes
-

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
-
Arabidopsis thaliana
-
leaf
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence Arabidopsis thaliana ?
-
?
additional information 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 Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
homohexamer FtsH forms homohexameric ring structures and large heterocomplexes with HflK/C Escherichia coli
More chloroplast FtsH proteins form complexes, likely hexamers of 400-450 kDa. Most of these are heterocomplexes built by different FtsH isozymes Arabidopsis thaliana
More 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 Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
AtFtsH2
-
Arabidopsis thaliana
AtFtsH5
-
Arabidopsis thaliana
filamentation temperature sensitive H
-
Arabidopsis thaliana
FtsH
-
Escherichia coli
FtsH
-
Synechocystis sp.
FtsH
-
Arabidopsis thaliana
FtsH1
-
Arabidopsis thaliana
FtsH10
-
Arabidopsis thaliana
FtsH11
-
Arabidopsis thaliana
FtsH12
-
Arabidopsis thaliana
FtsH3
-
Arabidopsis thaliana
FtsH4
-
Arabidopsis thaliana
FtsH6
-
Arabidopsis thaliana
FtsH7
-
Arabidopsis thaliana
FtsH8
-
Arabidopsis thaliana
FtsH9
-
Arabidopsis thaliana
FTSHA
-
Arabidopsis thaliana
FtsHB
-
Arabidopsis thaliana
VAR1
-
Arabidopsis thaliana
VAR2
-
Arabidopsis thaliana

Expression

Organism Comment Expression
Arabidopsis thaliana ethyl methanesulfonate can cause loss-of-function mutations in gene var2, D1 degradation is impaired in var2 mutant additional information
Arabidopsis thaliana the knockout mutant of gene AtFtsH11 shows a phenotype susceptible to high temperature stress additional information

General Information

General Information Comment Organism
evolution FtsH gene multiplication is of adaptive value during the course of evolution of oxygenic photosynthesis Arabidopsis thaliana
additional information mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation Arabidopsis thaliana
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 Escherichia coli
physiological function in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins Arabidopsis thaliana
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 Synechocystis sp.
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 Arabidopsis thaliana
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 Arabidopsis thaliana