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PMID: 14973038 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Dimerization of the RamC morphogenetic protein of Streptomyces coelicolor.

Journal of bacteriology ·Vol. 186 ·No. 5 ·2004-03-00 ·Pages 1330-6

Hudson ME, Nodwell JR

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 approximately 0.1 micro M. These data suggest that RamC acts as a dimer in vivo.

MeSH Terms
Bacterial Proteins/chemistry,genetics,metabolism Base Sequence Dimerization Gene Dosage Gene Expression Regulation, Bacterial Molecular Sequence Data Morphogenesis Mutation Spores, Bacterial/physiology Streptomyces/genetics,growth & development,metabolism,physiology
Chemicals
Bacterial Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hudson Michael E
Department of Biochemistry, Health Sciences Centre, McMaster University, Hamilton, Ontario, Canada L8N 3Z5.
Nodwell Justin R
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.186.5.1330-1336.2004
Published
2004-03-00
Pages
1330-6
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC344429
Subset
IM
External Links
PubMed source DOI: 10.1128/JB.186.5.1330-1336.2004 PMC Full Text View journal details
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