Evidence map›Paper›PMID 20628047›Full record

ArticleThe Journal of biological chemistry2010

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

Stéphane T Gabilly, Beth Welty Dreyfuss, Mohamed Karamoko, Vincent Corvest, Janette Kropat, M Dudley Page, Sabeeha S Merchant, Patrice P Hamel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Regulation of Iron Homeostasis and Use in Chloroplasts.International journal of molecular sciences · 2020
    Review
  5. Article
  6. Article
  7. Maturation of PlastidFrontiers in plant science · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Regulatory factors for the assembly of thylakoid membrane protein complexes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

Stéphane T GabillyFrom the Department of Molecular Genetics and Department of Molecular Cellular Biochemistry and.
Beth Welty Dreyfuss
Mohamed Karamoko
Vincent Corvest
Janette Kropat
M Dudley Page
Sabeeha S Merchant
Patrice P Hamel
The Ohio State University · USCellular Research (United States) · USInstitute of Molecular Genetics · RU

Funding

MATURATION OF CHLOROPLAST CYTOCHROMESR01GM048350 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MERCHANT, SABEEHA · 1993 to 2001
$413k
ISOLATION OF GENES INVOLVED IN CYTOCHROME BIOGENESISF32GM017483 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DREYFUSS, BETH W · 1995 to 1997
–
NIGMS NIH HHS F32 GM017483NIGMS NIH HHS R01 GM048350
6 · The paper itself

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.

Indexed as

AnimalsArabidopsisArabidopsis ProteinsBinding SitesChlamydomonas reinhardtiiCytochromes cCytochromes c6Cytochromes fHemeMutationOxidation-ReductionProtozoan ProteinsThioredoxinsThylakoidsArabidopsis ProteinsCytochromes cCytochromes c6Cytochromes fHemeProtozoan ProteinsThioredoxins

Identifiers

PMID20628047
PMCPMC2943297
OpenAlexW2098857744

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.