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J Biol Chem. 2005 Jan 7;280(1):236-43. Epub 2004 Oct 28.

CcmD is involved in complex formation between CcmC and the heme chaperone CcmE during cytochrome c maturation.

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  • 1Institut für Mikrobiologie, Eidgenössische Technische Hochschule, Wolfgang-Pauli-Str. 10, CH-8093 Zürich, Switzerland.

Abstract

CcmD is a small membrane protein involved in heme delivery to the heme chaperone CcmE during cytochrome c maturation. Here we show that it physically interacts with CcmE and CcmC, another essential component of the heme delivery system. We demonstrate the formation of a ternary complex consisting of CcmCDE. A deletion analysis of individual domains revealed that the central hydrophobic domain is essential for its function. Moreover, the C-terminal, cytoplasmic domain seems to require a net positive charge to be functional. Our topology analysis indicates that CcmD is an integral interfacial membrane protein with its N and C termini extruding into the cytoplasmic side of the membrane. Interactions of CcmD with either ferrochelatase, the last heme biosynthetic enzyme, or directly with heme were not detectable. We postulate a function for CcmD in protein-protein interaction or membrane protein assembly required for the heme delivery process.

PMID:
15513913
[PubMed - indexed for MEDLINE]
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