Dimerization of the RamC Morphogenetic Protein of Streptomyces coelicolor

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Abstract
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 K d of ∼0.1 μM. These data suggest that RamC acts as a dimer in vivo.