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Journal of Bacteriology, July 2003, p. 3821-3827, Vol. 185, No. 13
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.13.3821-3827.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The C-Terminal Flexible Domain of the Heme Chaperone CcmE Is Important but Not Essential for Its Function

Elisabeth Enggist and Linda Thöny-Meyer*

Institut für Mikrobiologie, Departement Biologie, Eidgenössische Technische Hochschule, CH-8092 Zürich, Switzerland

Received 28 February 2003/ Accepted 17 April 2003

CcmE is a heme chaperone active in the cytochrome c maturation pathway of Escherichia coli. It first binds heme covalently to strictly conserved histidine H130 and subsequently delivers it to apo-cytochrome c. The recently solved structure of soluble CcmE revealed a compact core consisting of a ß-barrel and a flexible C-terminal domain with a short {alpha}-helical turn. In order to elucidate the function of this poorly conserved domain, CcmE was truncated stepwise from the C terminus. Removal of all 29 amino acids up to crucial histidine 130 did not abolish heme binding completely. For detectable transfer of heme to type c cytochromes, only one additional residue, D131, was required, and for efficient cytochrome c maturation, the seven-residue sequence 131DENYTPP137 was required. When soluble forms of CcmE were expressed in the periplasm, the C-terminal domain had to be slightly longer to allow detection of holo-CcmE. Soluble full-length CcmE had low activity in cytochrome c maturation, indicating the importance of the N-terminal membrane anchor for the in vivo function of CcmE.

* Corresponding author. Mailing address: Institut für Mikrobiologie, Departement Biologie, Eidgenössische Technische Hochschule, Schmelzbergstrasse 7, CH-8092 Zürich, Switzerland. Phone: 41-1-632-3326. Fax: 41-1-632-1148. E-mail: lthoeny{at}micro.biol.ethz.ch.

Journal of Bacteriology, July 2003, p. 3821-3827, Vol. 185, No. 13
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.13.3821-3827.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Dale, J. R., Wade, R. Jr., DiChristina, T. J. (2007). A Conserved Histidine in Cytochrome c Maturation Permease CcmB of Shewanella putrefaciens Is Required for Anaerobic Growth below a Threshold Standard Redox Potential. J. Bacteriol. 189: 1036-1043 [Abstract] [Full Text]  
  • Stevens, J. M., Uchida, T., Daltrop, O., Kitagawa, T., Ferguson, S. J. (2006). Dynamic Ligation Properties of the Escherichia coli Heme Chaperone CcmE to Non-covalently Bound Heme. J. Biol. Chem. 281: 6144-6151 [Abstract] [Full Text]  
  • Harvat, E. M., Stevens, J. M., Redfield, C., Ferguson, S. J. (2005). Functional Characterization of the C-terminal Domain of the Cytochrome c Maturation Protein CcmE. J. Biol. Chem. 280: 36747-36753 [Abstract] [Full Text]  


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