Involvement of an FtsH homologue in the assembly of functional photosystem I in the cyanobacterium <i>Synechocystis</i> sp. PCC 6803

Mann, Nicholas H.; Novac, Natalia; Mullineaux, Conrad W.; Newman, Julie; Bailey, Shaun; Robinson, Colin

doi:10.1016/s0014-5793(00)01871-8

Cited by 91 publications

(94 citation statements)

References 39 publications

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“…Synechocystis also contains four FtsHs (Mann et al, 2000). This may reflect the need for thylakoid membranes to repair their protein complexes as a result of damage incurred by changing environmental conditions or to remodulate their protein composition during the development of different types of plastids.…”

Section: The Ftsh Protein Family In Higher Plantsmentioning

confidence: 99%

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

et al. 2003

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Arabidopsis YELLOW VARIEGATED1 ( VAR1 ) and VAR2 are separate loci that encode similar chloroplast FtsH proteases. To date, FtsH is the best-characterized protease in thylakoid membranes involved in the turnover of photosynthetic protein complexes. It comprises a protein family that is encoded by 12 different nuclear genes in Arabidopsis. We show here that nine FtsH proteins are located in the chloroplasts. Mutations in either VAR1 or VAR2 cause typical leaf variegation and sensitivity to photoinhibition. By contrast, none of these phenotypes was observed in T-DNA insertion mutants in other ftsH genes ( ftsh1 , ftsh6 , and ftsh8 ) closely related to VAR1 and VAR2 . This finding suggests that VAR1 and VAR2 play a predominant role in the photosystem II repair cycle in thylakoid membranes. By generating VAR1-and VAR2-specific antibodies, we found that loss of either VAR1 or VAR2 results in the decreased accumulation of the other. Thus, the genetic nonredundancy between VAR1 and VAR2 could be attributed to their coordinated regulation at the protein level. These observations led us to examine whether VAR1 and VAR2 form a complex. Sucrose density gradient and gel filtration analyses revealed a complex of ‫ف‬ 400 to 450 kD, probably representing a hexamer. Furthermore, VAR1 and VAR2 were shown to coprecipitate by immunoprecipitation using VAR1-and VAR2-specific antibodies. The majority of VAR1 appears to exist as heterocomplexes with VAR2, whereas VAR2 may be present as homocomplexes as well. Based on these results, we conclude that VAR1 and VAR2 are the major components of an FtsH complex involved in the repair of photodamaged proteins in thylakoid membranes.

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Section: The Ftsh Protein Family In Higher Plantsmentioning

confidence: 99%

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

et al. 2003

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“…In the case of the cyanobacterium Synechocystis sp PCC 6803 (hereafter Synechocystis 6803), four FtsH homologs, designated FtsH1-4, encoded by slr1390, slr0228, slr1604, and sll1463, respectively, have been identified from analysis of the genome sequence (Mann et al, 2000). FtsH2 and FtsH4 are dispensable, whereas FtsH1 and FtsH3 are required for cell viability (Mann et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…FtsH2 and FtsH4 are dispensable, whereas FtsH1 and FtsH3 are required for cell viability (Mann et al, 2000). Studies on mutants lacking FtsH2 have provided compelling evidence for a physiological role for this FtsH subunit in the degradation of D1 during PSII repair in vivo (Silva et al, 2003;Komenda et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Subunit Organization of a Synechocystis Hetero-Oligomeric Thylakoid FtsH Complex Involved in Photosystem II Repair

Boehm

Krynická

et al. 2012

The Plant Cell

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FtsH metalloproteases are key components of the photosystem II (PSII) repair cycle, which operates to maintain photosynthetic activity in the light. Despite their physiological importance, the structure and subunit composition of thylakoid FtsH complexes remain uncertain. Mutagenesis has previously revealed that the four FtsH homologs encoded by the cyanobacterium Synechocystis sp PCC 6803 are functionally different: FtsH1 and FtsH3 are required for cell viability, whereas FtsH2 and FtsH4 are dispensable. To gain insights into FtsH2, which is involved in selective D1 protein degradation during PSII repair, we used a strain of Synechocystis 6803 expressing a glutathione S-transferase (GST)-tagged derivative (FtsH2-GST) to isolate FtsH2-containing complexes. Biochemical analysis revealed that FtsH2-GST forms a hetero-oligomeric complex with FtsH3. FtsH2 also interacts with FtsH3 in the wild-type strain, and a mutant depleted in FtsH3, like ftsH2 2 mutants, displays impaired D1 degradation. FtsH3 also forms a separate heterocomplex with FtsH1, thus explaining why FtsH3 is more important than FtsH2 for cell viability. We investigated the structure of the isolated FtsH2-GST/FtsH3 complex using transmission electron microscopy and single-particle analysis. The three-dimensional structural model obtained at a resolution of 26 Å revealed that the complex is hexameric and consists of alternating FtsH2/FtsH3 subunits.

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“…This bidirectionality in the processive digestion makes it possible for FtsH to promptly degrade unnecessary membrane proteins. FtsH genes exist not only in bacteria but also in photosynthetic organisms, such as cyanobacteria and higher plants [67][68][69]. An FtsH homolog in higher plants was first found by an immunological analysis with an antibody against E. coli FtsH protease, which was shown to cross-react with a protein in spinach thylakoid membranes [70].…”

Section: Molecular Structure and General Function Of Ftsh Proteasesmentioning

confidence: 99%

“…PCC6803, where four genes slr1390, slr0228, slr1604 and sll1463 were found to be homologous to the bacterial FtsH (FtsH1, 2, 3 and 4) [45,69,72]. Of the four homologs, FtsH1 and 3 are required for cell viability while FtsH2 and 4 are not essential for the survival of the cyanobacterium [68,69].…”

Section: Specific Roles Of Ftsh Proteases In the Cyanobacteria And Chmentioning

confidence: 99%

Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

Yoshioka-Nishimura

Yamamoto

2014

Journal of Photochemistry and Photobiology B: Biology

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The reaction center-binding D1 protein of Photosystem II is damaged by excessive light, which leads to photoinhibition of Photosystem II. The damaged D1 protein is removed immediately by specific proteases, and a metalloprotease FtsH located in the thylakoid membranes is involved in the proteolytic process. According to recent studies on the distribution and organization of the protein complexes/supercomplexes in the thylakoid membranes, the grana of higher plant chloroplasts are crowded with Photosystem II complexes and light-harvesting complexes. For the repair of the photodamaged D1 protein, the majority of the active hexameric FtsH proteases should be localized in close proximity to the Photosystem II complexes. The unstacking of the grana may increase the area of the grana margin and facilitate easier access of the FtsH proteases to the damaged D1 protein. These results suggest that the structural changes of the thylakoid membranes by light stress increase the mobility of the membrane proteins and support the quality control of Photosystem II. (159 words)

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Involvement of an FtsH homologue in the assembly of functional photosystem I in the cyanobacterium Synechocystis sp. PCC 6803

Cited by 91 publications

References 39 publications

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

Subunit Organization of a Synechocystis Hetero-Oligomeric Thylakoid FtsH Complex Involved in Photosystem II Repair

Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

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