Evidence map›Paper›PMID 18753134›Full record

ArticleThe Journal of biological chemistry2008

The cytochrome c maturation components CcmF, CcmH, and CcmI form a membrane-integral multisubunit heme ligation complex.

Carsten Sanders, Serdar Turkarslan, Dong-Woo Lee, Ozlem Onder, Robert G Kranz, Fevzi Daldal

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. A redox- and proton-coupled inner membrane transporter mediates copper import to the bacterial cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Mitochondrial small heat shock protein mediates seed germination via thermal sensing.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. The CcmC-CcmE interaction during cytochromeThe Journal of biological chemistry · 2018
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  11. Article
  12. Review
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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.

Carsten SandersDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Serdar Turkarslan
Dong-Woo Lee
Ozlem Onder
Robert G Kranz
Fevzi Daldal

Funding

MOLECULAR GENETIC ANALYSES OF CYTOCHROMES C BIOGENESISR01GM047909 · NIGMS · WASHINGTON UNIVERSITY · PI KRANZ, ROBERT G. · 1994 to 2019
$6.0M
Respiratory Complex III: Supercomplexes and ROS, from Bacteria to HumanR01GM038237 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DALDAL, M. FEVZI · 1987 to 2018
$5.9M
CYTOCHROMES C BIOGENESISR55GM047909 · NIGMS · WASHINGTON UNIVERSITY · PI KRANZ, ROBERT G. · 1992 to 1992
–
NIGMS NIH HHS GM38237NIGMS NIH HHS GM47909NIGMS NIH HHS R01 GM038237
6 · The paper itself

Abstract

Cytochrome c maturation (Ccm) is a post-translational and post-export protein modification process that involves ten (CcmABCDEFGHI and CcdA or DsbD) components in most Gram-negative bacteria. The absence of any of these components abolishes the ability of cells to form cytochrome c, leading in the case of Rhodobacter capsulatus to the loss of photosynthetic proficiency and respiratory cytochrome oxidase activity. Based on earlier molecular genetic studies, we inferred that R. capsulatus CcmF, CcmH, and CcmI interact with each other to perform heme-apocytochrome c ligation. Here, using functional epitope-tagged derivatives of these components coproduced in appropriate mutant strains, we determined protein-protein interactions between them in detergent-dispersed membranes. Reciprocal affinity purification as well as tandem size exclusion and affinity chromatography analyses provided the first biochemical evidence that CcmF, CcmH, and CcmI associate stably with each other, indicating that these Ccm components form a membrane-integral complex. Under the conditions used, the CcmFHI complex does not contain CcmG, suggesting that the latter thio-reduction component is not always associated with the heme ligation components. The findings are discussed with respect to defining the obligatory components of a minimalistic heme-apocytochrome c ligation complex in R. capsulatus.

Indexed as

Cell MembraneChromatographyChromatography, AffinityCytochromes cDetergentsEpitopesGenetic TechniquesHemeModels, BiologicalMultiprotein ComplexesMutationPhotosynthesisPlasmidsProtein Structure, TertiaryRhodobacter capsulatusCytochromes cDetergentsEpitopesHemeMultiprotein Complexes

Identifiers

PMID18753134
PMCPMC2573057

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.