CCS5, a thioredoxin-like protein involved in the assembly of plastid c-type cytochromes.

The Journal of Biological Chemistry
Stéphane T GabillyPatrice P Hamel

Abstract

The c-type cytochromes are metalloproteins with a heme molecule covalently linked to the sulfhydryls of a CXXCH heme-binding site. In plastids, at least six assembly factors are required for heme attachment to the apo-forms of cytochrome f and cytochrome c(6) in the thylakoid lumen. CCS5, controlling plastid cytochrome c assembly, was identified through insertional mutagenesis in the unicellular green alga Chlamydomonas reinhardtii. The complementing gene encodes a protein with similarity to Arabidopsis thaliana HCF164, which is a thylakoid membrane-anchored protein with a lumen-facing thioredoxin-like domain. HCF164 is required for cytochrome b(6)f biogenesis, but its activity and site of action in the assembly process has so far remained undeciphered. We show that CCS5 is a component of a trans-thylakoid redox pathway and operates by reducing the CXXCH heme-binding site of apocytochrome c prior to the heme ligation reaction. The proposal is based on the following findings: 1) the ccs5 mutant is rescued by exogenous thiols; 2) CCS5 interacts with apocytochrome f and c(6) in a yeast two-hybrid assay; and 3) recombinant CCS5 is able to reduce a disulfide in the CXXCH heme-binding site of apocytochrome f.

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Citations

Apr 26, 2012·Antioxidants & Redox Signaling·Yves MeyerChristophe Riondet
Nov 14, 2012·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Wei ChiLixin Zhang
Oct 1, 2011·The FEBS Journal·Jörg Simon, Lars Hederstedt
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Sep 20, 2018·The New Phytologist·Andreas J MeyerNicolas Rouhier
May 15, 2020·International Journal of Molecular Sciences·Gretchen E Kroh, Marinus Pilon
Aug 12, 2017·Frontiers in Plant Science·Stéphane T Gabilly, Patrice P Hamel

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