Evidence map›Paper›PMID 20697122›Full record

ArticleGenetics2010

c-type cytochrome assembly in Saccharomyces cerevisiae: a key residue for apocytochrome c1/lyase interaction.

Vincent Corvest, Darren A Murrey, Delphine G Bernard, David B Knaff, Bernard Guiard, Patrice P Hamel

Open access · bronzeAbstract read
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Article in Genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

Vincent CorvestDepartment of Chemistry and Biochemistry, Center for Biotechnology and Genomics, Texas Tech University, Lubbock, TX 79409, USA.
Darren A Murrey
Delphine G Bernard
David B Knaff
Bernard Guiard
Patrice P Hamel
The Ohio State University · USCentre de Génétique Moléculaire · FRTexas Tech University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The electron transport chains in the membranes of bacteria and organelles generate proton-motive force essential for ATP production. The c-type cytochromes, defined by the covalent attachment of heme to a CXXCH motif, are key electron carriers in these energy-transducing membranes. In mitochondria, cytochromes c and c(1) are assembled by the cytochrome c heme lyases (CCHL and CC(1)HL) and by Cyc2p, a putative redox protein. A cytochrome c(1) mutant with a CAPCH heme-binding site instead of the wild-type CAACH is strictly dependent upon Cyc2p for assembly. In this context, we found that overexpression of CC(1)HL, as well as mutations of the proline in the CAPCH site to H, L, S, or T residues, can bypass the absence of Cyc2p. The P mutation was postulated to shift the CXXCH motif to an oxidized form, which must be reduced in a Cyc2p-dependent reaction before heme ligation. However, measurement of the redox midpoint potential of apocytochrome c(1) indicates that neither the P nor the T residues impact the thermodynamic propensity of the CXXCH motif to occur in a disulfide vs. dithiol form. We show instead that the identity of the second intervening residue in the CXXCH motif is key in determining the CCHL-dependent vs. CC(1)HL-dependent assembly of holocytochrome c(1). We also provide evidence that Cyc2p is dedicated to the CCHL pathway and is not required for the CC(1)HL-dependent assembly of cytochrome c(1).

Indexed as

Binding SitesCarrier ProteinsCytochromes cElectron TransportElectrophoresis, Polyacrylamide GelGene Expression Regulation, FungalHemeLyasesMitochondriaMitochondrial ProteinsMutationOxidation-ReductionPolymerase Chain ReactionSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsCYC2 protein, S cerevisiaecytochrome C synthetaseCytochromes cHemeLyasesMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID20697122
PMCPMC2954471
OpenAlexW2103510671

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.