Cited by 85Bacterial Genetics and BiotechnologyMetalloenzymes and iron-sulfur proteinsHeat shock proteins research

ABC transporter‐mediated release of a haem chaperone allows cytochrome c biogenesis

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Feissner, Robert E., Richard‐Fogal, Cynthia L., Frawley, Elaine R., Kranz, Robert G.·2006·Molecular Microbiology

Abstract

Summary: Although organisms from all kingdoms have either the system I or II cytochrome c biogenesis pathway, it has remained a mystery as to why these two distinct pathways have developed. We have previously shown evidence that the system I pathway has a higher affinity for haem than system II for cytochrome c biogenesis. Here, we show the mechanism by which the system I pathway can utilize haem at low levels. The mechanism involves an ATP‐binding cassette (ABC) transporter that is required for release of the periplasmic haem chaperone CcmE to the last step of cytochrome c assembly. This ABC transporter is composed of the ABC subunit CcmA, and two membrane proteins, CcmB and CcmC. In the absence of CcmA or CcmB, holo(haem)CcmE binds to CcmC in a stable dead‐end complex, indicating high affinity binding of haem to CcmC. Expression of CcmA and CcmB facilitates formation of the CcmA 2 B 1 C 1 complex and ATP‐dependent release of holoCcmE. We propose that the CcmA 2 B 1 C 1 complex represents a new subgroup within the ABC transporter superfamily that functions to release a chaperone.

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Crossref · 10.1111/j.1365-2958.2006.05221.x

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Authors
Feissner, R. E., Richard‐Fogal, C. L., Frawley, E. R., & Kranz, R. G.
Affiliations
Washington University in St. Louis (US)
Corresponding author
Kranz, Robert G.
Venue
Molecular Microbiology
Publisher
Wiley
Published
2006-05-30
Volume
61
Issue
1
Pages
219-231
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
OpenAlex
W1501758551
Cited by
85
References
56
Citations by year
2026: 3 · 2025: 4 · 2024: 2 · 2023: 4 · 2022: 4 · 2021: 2 · 2020: 2 · 2019: 1 · 2018: 4 · 2016: 4 · 2015: 3 · 2014: 3 · 2013: 5 · 2012: 5
FWCI
4.73
Type
journal article
Language
en
Open access
Locations
  • Molecular Microbiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (GM 47909)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords
cytochrome c biogenesis, ABC transporters, CCMA, CCMC, heme binding, periplasmic chaperone
MeSH terms
Apoproteins, Bacterial Outer Membrane Proteins, Bacterial Proteins, Biological Transport, Cytochrome c Group, Escherichia coli, Heme, Hemeproteins, Membrane Proteins, Models, Biological, Plasmids, Recombinant Fusion Proteins, ATP-Binding Cassette Transporters, Molecular Chaperones, Escherichia coli Proteins

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