skip to main content
DOE PAGES title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid Cytochrome c Assembly in the Green Alga Chlamydomonas reinhardtii

Abstract

In bacteria and energy generating organelles, c-type cytochromes are a class of universal electron carriers with a heme cofactor covalently linked via one or two thioether bonds to a heme binding site. The covalent attachment of heme to apocytochromes is a catalyzed process, taking place via three evolutionarily distinct assembly pathways (Systems I, II, III). System II was discovered in the green alga Chlamydomonas reinhardtii through the genetic analysis of the ccs mutants (cytochrome c synthesis), which display a block in the apo- to holo- form conversion of cytochrome f and c6, the thylakoid lumen resident c-type cytochromes functioning in photosynthesis. Here we show that the gene corresponding to the CCS2 locus encodes a 1,719 amino acid polypeptide and identify the molecular lesions in the ccs2-1 to ccs2-5 alleles. The CCS2 protein displays seven degenerate amino acid repeats, which are variations of the octatricopeptide-repeat motif (OPR) recently recognized in several nuclear-encoded proteins controlling the maturation, stability, or translation of chloroplast transcripts. A plastid site of action for CCS2 is inferred from the finding that GFP fused to the first 100 amino acids of the algal protein localizes to chloroplasts in Nicotiana benthamiana. Here, we discuss the possible functions of CCS2more » in the heme attachment reaction.« less

Authors:
 [1];  [2];  [3]
  1. The Ohio State Univ., Columbus, OH (United States). Dept. of Molecular Genetics, Dept. of Biological Chemistry and Pharmacology, and Plant Cellular and Molecular Biology Graduate Program; Athens State Univ., Athens, AL (United States). Dept. of Mathematics, Computer and Natural Sciences
  2. The Ohio State Univ., Columbus, OH (United States). Dept. of Molecular Genetics, Dept. of Biological Chemistry and Pharmacology
  3. The Ohio State Univ., Columbus, OH (United States). Dept. of Molecular Genetics, Dept. of Biological Chemistry and Pharmacology, and Plant Cellular and Molecular Biology Graduate Program
Publication Date:
Research Org.:
The Ohio State Univ., Columbus, OH (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1463691
Grant/Contract Number:  
SC0014562
Resource Type:
Accepted Manuscript
Journal Name:
Frontiers in Plant Science
Additional Journal Information:
Journal Volume: 8; Journal ID: ISSN 1664-462X
Publisher:
Frontiers Research Foundation
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; plastid; photosynthesis; cytochrome c; heme; assembly factor; OPR

Citation Formats

Cline, Sara G., Laughbaum, Isaac A., and Hamel, Patrice P. CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid Cytochrome c Assembly in the Green Alga Chlamydomonas reinhardtii. United States: N. p., 2017. Web. doi:10.3389/fpls.2017.01306.
Cline, Sara G., Laughbaum, Isaac A., & Hamel, Patrice P. CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid Cytochrome c Assembly in the Green Alga Chlamydomonas reinhardtii. United States. doi:10.3389/fpls.2017.01306.
Cline, Sara G., Laughbaum, Isaac A., and Hamel, Patrice P. Thu . "CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid Cytochrome c Assembly in the Green Alga Chlamydomonas reinhardtii". United States. doi:10.3389/fpls.2017.01306. https://www.osti.gov/servlets/purl/1463691.
@article{osti_1463691,
title = {CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid Cytochrome c Assembly in the Green Alga Chlamydomonas reinhardtii},
author = {Cline, Sara G. and Laughbaum, Isaac A. and Hamel, Patrice P.},
abstractNote = {In bacteria and energy generating organelles, c-type cytochromes are a class of universal electron carriers with a heme cofactor covalently linked via one or two thioether bonds to a heme binding site. The covalent attachment of heme to apocytochromes is a catalyzed process, taking place via three evolutionarily distinct assembly pathways (Systems I, II, III). System II was discovered in the green alga Chlamydomonas reinhardtii through the genetic analysis of the ccs mutants (cytochrome c synthesis), which display a block in the apo- to holo- form conversion of cytochrome f and c6, the thylakoid lumen resident c-type cytochromes functioning in photosynthesis. Here we show that the gene corresponding to the CCS2 locus encodes a 1,719 amino acid polypeptide and identify the molecular lesions in the ccs2-1 to ccs2-5 alleles. The CCS2 protein displays seven degenerate amino acid repeats, which are variations of the octatricopeptide-repeat motif (OPR) recently recognized in several nuclear-encoded proteins controlling the maturation, stability, or translation of chloroplast transcripts. A plastid site of action for CCS2 is inferred from the finding that GFP fused to the first 100 amino acids of the algal protein localizes to chloroplasts in Nicotiana benthamiana. Here, we discuss the possible functions of CCS2 in the heme attachment reaction.},
doi = {10.3389/fpls.2017.01306},
journal = {Frontiers in Plant Science},
number = ,
volume = 8,
place = {United States},
year = {2017},
month = {8}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 1 work
Citation information provided by
Web of Science

Save / Share:

Works referenced in this record:

GATEWAY™ vectors for Agrobacterium-mediated plant transformation
journal, May 2002


WebLogo: A Sequence Logo Generator
journal, May 2004

  • Crooks, Gavin E.; Hon, Gary; Chandonia, John-Marc
  • Genome Research, Vol. 14, Issue 6, p. 1188-1190
  • DOI: 10.1101/gr.849004