Topology and function of CcmD in cytochrome c maturation

J Bacteriol. 2008 May;190(10):3489-93. doi: 10.1128/JB.00146-08. Epub 2008 Mar 7.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / physiology*
  • Biological Transport
  • Cell Membrane
  • Cytochromes c / biosynthesis*
  • Cytochromes c / chemistry
  • Cytochromes c / metabolism*
  • Escherichia coli / genetics*
  • Escherichia coli / growth & development
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Genes, Bacterial
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology*

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • CcmC protein, bacteria
  • CcmD protein, E coli
  • Escherichia coli Proteins
  • Membrane Proteins
  • Cytochromes c