The carboxyl-terminal processing of precursor D1 protein of the photosystem II reaction center

Satoh, Kimiyuki; Yamamoto, Yasutake

doi:10.1007/s11120-007-9191-z

Cited by 40 publications

(50 citation statements)

References 77 publications

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“…In Arabidopsis thaliana, three genes (At4g17740, At3g57680, and At5g46390) are predicted to encode Ctp homologs according to amino acid sequence homology analysis (5,10). Initially, we compared the cyanobacterial CtpA with these three Arabidopsis Ctp proteins and found that it shared 42%, 36%, and 31% amino acid identity with At4g17740, At3g57680, and At5g46390, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…The C-terminal tail of pD1 must be cleaved by an endopeptidase named the carboxyl terminal peptidase (Ctp) to produce mature D1, the functional form (5). In the cyanobacterium Synechocystis PCC 6803, there are three Ctp homologs (CtpA, CtpB, and CtpC), but only one, CtpA, is responsible for cleavage of the pD1 C-terminal extension (5). Disruption of CtpA leads to a loss of PSII activity and oxygen evolution from failure to form the manganese cluster (4,6).…”

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confidence: 99%

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C-terminal processing of reaction center protein D1 is essential for the function and assembly of photosystem II inArabidopsis

Che

Hou³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Photosystem II (PSII) reaction center protein D1 is synthesized as a precursor (pD1) with a short C-terminal extension. The pD1 is processed to mature D1 by carboxyl-terminal peptidase A to remove the C-terminal extension and form active protein. Here we report functional characterization of the Arabidopsis gene encoding D1 C-terminal processing enzyme (AtCtpA) in the chloroplast thylakoid lumen. Recombinant AtCtpA converted pD1 to mature D1 and a mutant lacking AtCtpA retained all D1 in precursor form, confirming that AtCtpA is solely responsible for processing. As with cyanobacterial ctpa, a knockout Arabidopsis atctpa mutant was lethal under normal growth conditions but was viable with sucrose under low-light conditions. Viable plants, however, showed deficiencies in PSII and thylakoid stacking. Surprisingly, unlike its cyanobacterial counterpart, the Arabidopsis mutant retained both monomer and dimer forms of the PSII complexes that, although nonfunctional, contained both the core and extrinsic subunits. This mutant was also essentially devoid of PSII supercomplexes, providing an unexpected link between D1 maturation and supercomplex assembly. A knock-down mutant expressing about 2% wild-type level of AtCtpA showed normal growth under low light but was stunted and accumulated pD1 under high light, indicative of delayed C-terminal processing. Although demonstrating the functional significance of C-terminal D1 processing in PSII biogenesis, our study reveals an unsuspected link between D1 maturation and PSII supercomplex assembly in land plants, opening an avenue for exploring the mechanism for the association of light-harvesting complexes with the PSII core complexes.photosynthesis | photoinhibition P hotosystem II (PSII) consists of more than 20 subunits. Assembly of this photosystem is a multistep process that functions in a highly coordinated fashion (1-3). The process starts with PSII initiation complexes (D2, PsbE, PsbF, and PsbI), and then D1 and CP47 are sequentially recruited to form CP47-RC complexes, followed by addition of PsbH, PsbM, PsbTc, and PsbR subunits. Next, CP43 and other subunits are added to generate PSII monomers, which develop into PSII dimers. Finally, lightharvesting complex (LHC) II is attached to form PSII supercomplexes. The D1 protein of PSII is prone to photodamage under excessive light conditions (4). To sustain photosynthesis, damaged D1 protein is degraded and replaced with a newly synthesized copy via PSII repair-a highly complex and critical process whose mechanism remains unclear (3, 4).In most oxygen-evolving photosynthetic organisms, D1 protein is synthesized as a precursor (pD1) with a C-terminal tail. The pD1 protein is integrated into the thylakoid membrane and forms the initial PSII reaction center combined with other PSII

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

C-terminal processing of reaction center protein D1 is essential for the function and assembly of photosystem II inArabidopsis

Che

Hou³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…C-terminal processing protease, a monomeric Sertype protease that cleaves off a C-terminal extension for maturation of the D1 precursor protein, is another type of processing peptidase in the thylakoid lumen (Anbudurai et al, 1994;Fujita et al, 1995;Oelmüller et al, 1996;Satoh and Yamamoto, 2007;Che et al, 2013). Its basic structure contains a PDZ domain for D1 C-terminal binding and a protease domain with an SK dyad for proteolysis (Liao et al, 2000).…”

Section: Processing 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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“…CtpA cleaves the C-terminal extension, transforming pD1 into the mature, functional D1 (for a review of D1 processing, see Ref. 48). Processing of pD1 by CtpA to yield D1 is a critical step in PSII assembly and is a requirement for the binding of the catalytic Mn 4 CaO 5 cluster, the site of water oxidation (13).…”

Section: Primer Namementioning

confidence: 99%

An Atypical psbA Gene Encodes a Sentinel D1 Protein to Form a Physiologically Relevant Inactive Photosystem II Complex in Cyanobacteria

Wegener¹,

Nagarajan²,

Pakrasi

2015

Journal of Biological Chemistry

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Background: Unicellular cyanobacteria separate photosynthesis and nitrogen fixation using a day-night cycle. Results: Cyanothece 51142 expresses a D1 protein exclusively in the dark period that assembles nonfunctional photosystem II. Conclusion:The unusual D1 is named sentinel D1 because it prevents photosynthesis from occurring during nitrogen fixation. Significance: Expression of sentinel D1 allows photosynthesis and nitrogen fixation to coexist in the cell.

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The carboxyl-terminal processing of precursor D1 protein of the photosystem II reaction center

Cited by 40 publications

References 77 publications

C-terminal processing of reaction center protein D1 is essential for the function and assembly of photosystem II inArabidopsis

C-terminal processing of reaction center protein D1 is essential for the function and assembly of photosystem II inArabidopsis

Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments

An Atypical psbA Gene Encodes a Sentinel D1 Protein to Form a Physiologically Relevant Inactive Photosystem II Complex in Cyanobacteria

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