Dimerization of the RamC Morphogenetic Protein of Streptomyces coelicolor
2004 ◽
Vol 186
(5)
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pp. 1330-1336
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Keyword(s):
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 Kd of ∼0.1 μM. These data suggest that RamC acts as a dimer in vivo.
2002 ◽
Vol 184
(17)
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pp. 4920-4924
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2011 ◽
Vol 31
(47)
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pp. 16969-16976
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2004 ◽
Vol 24
(23)
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pp. 10397-10405
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2000 ◽
Vol 20
(9)
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pp. 3015-3026
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2004 ◽
Vol 24
(10)
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pp. 4502-4512
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