ABC transporter‐mediated release of a haem chaperone allows cytochrome c biogenesis
Open accessAbstract
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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The Ccm system I consists of two modules: module 1 includes CcmABCD and is responsible for acquiring and loading a heme molecule onto the heme chaperone CcmE.
“it is thought that the Ccm system I consists of two modules: module 1 includes CcmABCD and is responsible for acquiring and loading a heme molecule onto the heme chaperone CcmE43.”
From AF2Complex predicts direct physical interactions in multimeric proteins with deep learning (2022) · cites this paper as [43]
As previously proposed, the energy of ATP hydrolysis could be harnessed to release the cargo-loaded CcmE.
“As previously proposed43, the energy of the hydrolysis could be harnessed to release the cargo-loaded CcmE.”
From AF2Complex predicts direct physical interactions in multimeric proteins with deep learning (2022) · cites this paper as [43]
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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
- bronze
- doi.org
- 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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