Topology and function of CcmD in cytochrome C maturation

Cynthia L. Richard-Fogal; Elaine R. Frawley; Robert G. Kranz

doi:10.1128/JB.00146-08

Topology and function of CcmD in cytochrome C maturation

Cynthia L. Richard-Fogal, Elaine R. Frawley, Robert G. Kranz

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

The system I cytochrome c biogenesis pathway requires CcmD, a small polypeptide of 69 residues in Escherichia coli. Here it is shown that CcmD is a component of the CcmABC ATP-binding cassette transporter complex. CcmD is not necessary for the CcmC-dependent transfer of heme to CcmE in the periplasm or for interaction of CcmE with CcmABC. CcmD is absolutely required for the release of holo-CcmE from the CcmABCD complex. Evidence is presented that the topology of CcmD in the cytoplasmic membrane is the N terminus outside and the C terminus inside with one transmembrane domain.

Original language	English
Pages (from-to)	3489-3493
Number of pages	5
Journal	Journal of bacteriology
Volume	190
Issue number	10
DOIs	https://doi.org/10.1128/JB.00146-08
State	Published - May 2008

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AB - The system I cytochrome c biogenesis pathway requires CcmD, a small polypeptide of 69 residues in Escherichia coli. Here it is shown that CcmD is a component of the CcmABC ATP-binding cassette transporter complex. CcmD is not necessary for the CcmC-dependent transfer of heme to CcmE in the periplasm or for interaction of CcmE with CcmABC. CcmD is absolutely required for the release of holo-CcmE from the CcmABCD complex. Evidence is presented that the topology of CcmD in the cytoplasmic membrane is the N terminus outside and the C terminus inside with one transmembrane domain.

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Topology and function of CcmD in cytochrome C maturation

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