ArticleGenetics2011
A novel component of the disulfide-reducing pathway required for cytochrome c assembly in plastids.
Article in Genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Two disulfide-reducing pathways are required for the maturation of plastid c-type cytochromes in Chlamydomonas reinhardtii.Genetics · 2023Article
- Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7.Plant physiology · 2021Article
- The DnaJ-Like Zinc-Finger Protein HCF222 Is Required for Thylakoid Membrane Biogenesis in Plants.Plant physiology · 2017Article
- Maturation of PlastidFrontiers in plant science · 2017Review
- CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid CytochromeFrontiers in plant science · 2017Article
- Inducible Repression of Nuclear-Encoded Subunits of the Cytochrome b6f Complex in Tobacco Reveals an Extraordinarily Long Lifetime of the Complex.Plant physiology · 2014Article
- How to build functional thylakoid membranes: from plastid transcription to protein complex assembly.Planta · 2013Review
- Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis.Frontiers in plant science · 2013Article
- Regulatory factors for the assembly of thylakoid membrane protein complexes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis.The Plant cell · 2011Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
In plastids, the conversion of energy in the form of light to ATP requires key electron shuttles, the c-type cytochromes, which are defined by the covalent attachment of heme to a CXXCH motif. Plastid c-type cytochrome biogenesis occurs in the thylakoid lumen and requires a system for transmembrane transfer of reductants. Previously, CCDA and CCS5/HCF164, found in all plastid-containing organisms, have been proposed as two components of the disulfide-reducing pathway. In this work, we identify a small novel protein, CCS4, as a third component in this pathway. CCS4 was genetically identified in the green alga Chlamydomonas reinhardtii on the basis of the rescue of the ccs4 mutant, which is blocked in the synthesis of holoforms of plastid c-type cytochromes, namely cytochromes f and c(6). Although CCS4 does not display sequence motifs suggestive of redox or heme-binding function, biochemical and genetic complementation experiments suggest a role in the disulfide-reducing pathway required for heme attachment to apoforms of cytochromes c. Exogenous thiols partially rescue the growth phenotype of the ccs4 mutant concomitant with recovery of holocytochrome f accumulation, as does expression of an ectopic copy of the CCDA gene, encoding a trans-thylakoid transporter of reducing equivalents. We suggest that CCS4 might function to stabilize CCDA or regulate its activity.
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Registered trials
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