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Cloning and Expression of the Gene for a Novel Protein from Mycobacterium smegmatis with Functional Similarity to Eukaryotic Calmodulin

By Prasad T. Reddy, C. Rama Prasad, P. Hemalatha Reddy, Dennis Reeder, Keith McKenney, Howard Jaffe, Mariana N. Dimitrova, Ann Ginsburg, Alan Peterkofsky and P. Suryanarayana Murthy


A calmodulin-like protein (CAMLP) from Mycobacterium smegmatis was purified to homogeneity and partially sequenced; these data were used to produce a full-length clone, whose DNA sequence contained a 55-amino-acid open reading frame. M. smegmatis CAMLP, expressed in Escherichia coli, exhibited properties characteristic of eukaryotic calmodulin: calcium-dependent stimulation of eukaryotic phosphodiesterase, which was inhibited by the calmodulin antagonist trifluoperazine, and reaction with anti-bovine brain calmodulin antibodies. Consistent with the presence of nine acidic amino acids (16%) in M. smegmatis CAMLP, there is one putative calcium-binding domain in this CAMLP, compared to four such domains for eukaryotic calmodulin, reflecting the smaller molecular size (approximately 6 kDa) of M. smegmatis CAMLP. Ultracentrifugation and mass spectral studies excluded the possibility that calcium promotes oligomerization of purified M. smegmatis CAMLP

Topics: Physiology and Metabolism
Publisher: American Society for Microbiology
Year: 2003
DOI identifier: 10.1128/JB.185.17.5263-5268.2003
OAI identifier: oai:pubmedcentral.nih.gov:180971
Provided by: PubMed Central
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