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Journal of Bacteriology, March 2004, p. 1330-1336, Vol. 186, No. 5
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.5.1330-1336.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Dimerization of the RamC Morphogenetic Protein of Streptomyces coelicolor

Michael E. Hudson and Justin R. Nodwell*

Department of Biochemistry, Health Sciences Centre, McMaster University, Hamilton, Ontario, Canada L8N 3Z5

Received 1 October 2003/ Accepted 21 November 2003

RamC is required for the formation of spore-forming cells called aerial hyphae by the bacterium Streptomyces coelicolor. This protein is membrane associated and has an amino-terminal protein kinase-like domain, but little is known about its mechanism of action. In this study we found that the presence of multiple copies of a defective allele of ramC inhibits morphogenesis in S. coelicolor, consistent with either titration of a target or formation of inactive RamC multimers. We identified a domain in RamC that is C terminal to the putative kinase domain and forms a dimer with a Kd of ~0.1 µM. These data suggest that RamC acts as a dimer in vivo.

* Corresponding author. Mailing address: Department of Biochemistry, McMaster University, Health Sciences Centre, 1200 Main Street W., Hamilton, Ontario, Canada L8N 3Z5. Phone: (905) 525-9140, ext. 27335. Fax: (905) 522-9033. E-mail: nodwellj{at}mcmaster.ca.

Journal of Bacteriology, March 2004, p. 1330-1336, Vol. 186, No. 5
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.5.1330-1336.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Kodani, S., Hudson, M. E., Durrant, M. C., Buttner, M. J., Nodwell, J. R., Willey, J. M. (2004). From The Cover: The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor. Proc. Natl. Acad. Sci. USA 101: 11448-11453 [Abstract] [Full Text]  


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