FtsH proteases located in the plant chloroplast

Wagner, Raik; Aigner, Harald; Funk, Christiane

doi:10.1111/j.1399-3054.2011.01548.x

Cited by 106 publications

(129 citation statements)

References 79 publications

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“…AtFtsH7/9 found in the chloroplast envelope (Sakamoto et al 2003, Wagner et al 2012 are most closely related to cyanoFtsH4 whose function remains unclear. The FtsH-inactive subunit, AtFtsHi3, which only possesses the AAA+ domain, is phylogenetically close to AtFtsH7/9 and may have evolved through loss of the protease domain.…”

Section: Multiplicity Of Ftsh In Photosynthetic Eukaryotesmentioning

confidence: 99%

Early emergence of the FtsH proteases involved in photosystem II repair

Shao¹,

Cardona²,

Nixon³

2018

Photosynt.

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Efficient degradation of damaged D1 during the repair of PSII is carried out by a set of dedicated FtsH proteases in the thylakoid membrane. Here we investigated whether the evolution of FtsH could hold clues to the origin of oxygenic photosynthesis. A phylogenetic analysis of over 6000 FtsH protease sequences revealed that there are three major groups of FtsH proteases originating from gene duplication events in the last common ancestor of bacteria, and that 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. Furthermore, we showed that the phylogenetic tree of FtsH proteases in phototrophic bacteria is similar to that for Type I and Type II reaction centre proteins. We conclude that the phylogeny of FtsH proteases is consistent with an early origin of photosynthetic water oxidation chemistry.

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Section: Multiplicity Of Ftsh In Photosynthetic Eukaryotesmentioning

confidence: 99%

Early emergence of the FtsH proteases involved in photosystem II repair

Shao¹,

Cardona²,

Nixon³

2018

Photosynt.

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“…1; Wagner et al, 2012). FtsH7/9 share high sequence similarity and, therefore, have been speculated to constitute a heteromeric protease complex.…”

Section: Ftshmentioning

confidence: 99%

“…The other chloroplastic isomer, FtsH6, is dispensable for normal growth under high light and natural environmental stress conditions. However, its suborganellar location and precise function remain unclear (Wagner et al, 2012;Lu, 2016).…”

Section: Box 2 Architecture and Action Of The Processive Proteasesmentioning

confidence: 99%

Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments

2016

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ORCID IDs: 0000-0003-1718-9121 (Y.K.); 0000-0001-9747-5042 (W.S.).Chloroplasts originated from the endosymbiosis of ancestral cyanobacteria and maintain transcription and translation machineries for around 100 proteins. Most endosymbiont genes, however, have been transferred to the host nucleus, and the majority of the chloroplast proteome is composed of nucleus-encoded proteins that are biosynthesized in the cytosol and then imported into chloroplasts. How chloroplasts and the nucleus communicate to control the plastid proteome remains an important question. Protein-degrading machineries play key roles in chloroplast proteome biogenesis, remodeling, and maintenance. Research in the past few decades has revealed more than 20 chloroplast proteases, which are localized to specific suborganellar locations. In particular, two energy-dependent processive proteases of bacterial origin, Clp and FtsH, are central to protein homeostasis. Processing endopeptidases such as stromal processing peptidase and thylakoidal processing peptidase are involved in the maturation of precursor proteins imported into chloroplasts by cleaving off the amino-terminal transit peptides. Presequence peptidases and organellar oligopeptidase subsequently degrade the cleaved targeting peptides. Recent findings have indicated that not only intraplastidic but also extraplastidic processive protein-degrading systems participate in the regulation and quality control of protein translocation across the envelopes. In this review, we summarize current knowledge of the major chloroplast proteases in terms of type, suborganellar localization, and diversification. We present details of these degradation processes as case studies according to suborganellar compartment (envelope, stroma, and thylakoids). Key questions and future directions in this field are discussed.Over 1 billion years of plastid evolution since the endosymbiosis of ancestral cyanobacteria (Douzery et al., 2004), chloroplast biogenesis has gained complexity, with large sets of the endosymbiont genes being transferred to host nuclear genomes. While only 100 endosymbiont genes remain in the plastid genome, with the corresponding proteins biosynthesized there, the nuclear genes have often gained complexity by duplication and diversification of the original endosymbiotic genes. This complexity raises numerous questions regarding (1) at what level gene expression is coordinately controlled, (2) what molecules coordinate the cross talk between chloroplasts and the nucleus, (3) how proteins get across membranes and become imported into chloroplasts, and (4) how the stoichiometries of nucleus-and chloroplast-encoded subunits within individual chloroplast protein complexes such as photosystems and Rubisco are strictly maintained.Given these questions, chloroplast biogenesis has remained a central subject in plant physiology for the last few decades (Jarvis and López-Juez, 2013). In our view, the aforementioned questions point to the importance of protein homeostasis and posttranslational modificat...

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“…Four FtsH homologs (FtsH1 to FtsH4) are found in Synechocystis sp PCC 6803: FtsH3 copurifies with FtsH2 or FtsH1 in heterohexamers (Boehm et al, 2012). In Arabidopsis, the 12 nucleus-encoded FtsH family members (FtsH1 to FtsH12) are distributed between mitochondria and chloroplasts; in addition, five Arabidopsis FtsH-like proteins (FtsHi1 to FtsHi5) targeted to the chloroplast envelope lack the conserved zinc binding motif HisGluXxxXxxHis and are presumably inactive as protease (reviewed in Wagner et al, 2012; see also Arabidopsis proteome databases [Sun et al, 2009;Ferro et al, 2010]). Four isoforms have been identified in Arabidopsis thylakoid membranes: two of type A (FtsH1 and FtsH5) and two of type B (FtsH2 and FtsH8; Friso et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Thylakoid FtsH Protease Contributes to Photosystem II and Cytochromeb 6 fRemodeling inChlamydomonas reinhardtiiunder Stress Conditions

et al. 2014

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FtsH is the major thylakoid membrane protease found in organisms performing oxygenic photosynthesis. Here, we show that FtsH from Chlamydomonas reinhardtii forms heterooligomers comprising two subunits, FtsH1 and FtsH2. We characterized this protease using FtsH mutants that we identified through a genetic suppressor approach that restored phototrophic growth of mutants originally defective for cytochrome b 6 f accumulation. We thus extended the spectrum of FtsH substrates in the thylakoid membranes beyond photosystem II, showing the susceptibility of cytochrome b 6 f complexes (and proteins involved in the c i heme binding pathway to cytochrome b 6 ) to FtsH. We then show how FtsH is involved in the response of C. reinhardtii to macronutrient stress. Upon phosphorus starvation, photosynthesis inactivation results from an FtsH-sensitive photoinhibition process. In contrast, we identified an FtsH-dependent loss of photosystem II and cytochrome b 6 f complexes in darkness upon sulfur deprivation. The D1 fragmentation pattern observed in the latter condition was similar to that observed in photoinhibitory conditions, which points to a similar degradation pathway in these two widely different environmental conditions. Our experiments thus provide extensive evidence that FtsH plays a major role in the quality control of thylakoid membrane proteins and in the response of C. reinhardtii to light and macronutrient stress.

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FtsH proteases located in the plant chloroplast

Cited by 106 publications

References 79 publications

Early emergence of the FtsH proteases involved in photosystem II repair

Early emergence of the FtsH proteases involved in photosystem II repair

Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments

Thylakoid FtsH Protease Contributes to Photosystem II and Cytochromeb 6 fRemodeling inChlamydomonas reinhardtiiunder Stress Conditions

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