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Journal of Bacteriology, May 2008, p. 3489-3493, Vol. 190, No. 10
0021-9193/08/$08.00+0     doi:10.1128/JB.00146-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Topology and Function of CcmD in Cytochrome c Maturation{triangledown}

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

Department of Biology, Washington University, Campus Box 1137, 1 Brookings Drive, St. Louis, Missouri 63130

Received 28 January 2008/ Accepted 1 March 2008

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.

* Corresponding author. Mailing address: Department of Biology, Washington University, Campus Box 1137, 1 Brookings Drive, St. Louis, MO 63130. Phone: (314) 935-4278. Fax: (314) 935-4432. E-mail: kranz{at}biology.wustl.edu

{triangledown} Published ahead of print on 7 March 2008.

Journal of Bacteriology, May 2008, p. 3489-3493, Vol. 190, No. 10
0021-9193/08/$08.00+0     doi:10.1128/JB.00146-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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