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Journal of Bacteriology, June 2005, p. 4245-4256, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4245-4256.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Overproduction of CcmG and CcmFHRc Fully Suppresses the c-Type Cytochrome Biogenesis Defect of Rhodobacter capsulatus CcmI-Null Mutants

Carsten Sanders,1 Meenal Deshmukh,1,{dagger} Doniel Astor,1 Robert G. Kranz,2 and Fevzi Daldal1*

Department of Biology, Plant Science Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104,1 Department of Biology, Washington University, St. Louis, Missouri 631302

Received 12 January 2005/ Accepted 11 March 2005

Gram-negative bacteria like Rhodobacter capsulatus use intertwined pathways to carry out the posttranslational maturation of c-type cytochromes (Cyts). This periplasmic process requires at least 10 essential components for apo-Cyt c chaperoning, thio-oxidoreduction, and the delivery of heme and its covalent ligation. One of these components, CcmI (also called CycH), is thought to act as an apo-Cyt c chaperone. In R. capsulatus, CcmI-null mutants are unable to produce c-type Cyts and thus sustain photosynthetic (Ps) growth. Previously, we have shown that overproduction of the putative heme ligation components CcmF and CcmHRc (also called Ccl1 and Ccl2) can partially bypass the function of CcmI on minimal, but not on enriched, media. Here, we demonstrate that either additional overproduction of CcmG (also called HelX) or hyperproduction of CcmF-CcmHRc is needed to completely overcome the role of CcmI during the biogenesis of c-type Cyts on both minimal and enriched media. These findings indicate that, in the absence of CcmI, interactions between the heme ligation and thioreduction pathways become restricted for sufficient Cyt c production. We therefore suggest that CcmI, along with its apo-Cyt chaperoning function, is also critical for the efficacy of holo-Cyt c formation, possibly via its close interactions with other components performing the final heme ligation steps during Cyt c biogenesis.

* Corresponding author. Mailing address: Department of Biology, Plant Science Institute, University of Pennsylvania, Philadelphia, PA 19104. Phone: (215) 898-4394. Fax: (215) 898-8780. E-mail: fdaldal{at}sas.upenn.edu.

{dagger} Present address: Colgate-Palmolive Inc. Research Center, Piscataway, N.J.

Journal of Bacteriology, June 2005, p. 4245-4256, Vol. 187, No. 12
0021-9193/05/$08.00+0     doi:10.1128/JB.187.12.4245-4256.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kranz, R. G., Richard-Fogal, C., Taylor, J.-S., Frawley, E. R. (2009). Cytochrome c Biogenesis: Mechanisms for Covalent Modifications and Trafficking of Heme and for Heme-Iron Redox Control. Microbiol. Mol. Biol. Rev. 73: 510-528 [Abstract] [Full Text]  
  • Sanders, C., Turkarslan, S., Lee, D.-W., Onder, O., Kranz, R. G., Daldal, F. (2008). The Cytochrome c Maturation Components CcmF, CcmH, and CcmI Form a Membrane-integral Multisubunit Heme Ligation Complex. J. Biol. Chem. 283: 29715-29722 [Abstract] [Full Text]  
  • Sanders, C., Boulay, C., Daldal, F. (2007). Membrane-Spanning and Periplasmic Segments of CcmI Have Distinct Functions during Cytochrome c Biogenesis in Rhodobacter capsulatus. J. Bacteriol. 189: 789-800 [Abstract] [Full Text]  
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