Affordable Access

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

Authors
  • Prasad T. Reddy
  • C. Rama Prasad
  • P. Hemalatha Reddy
  • Dennis Reeder
  • Keith McKenney
  • Howard Jaffe
  • Mariana N. Dimitrova
  • Ann Ginsburg
  • Alan Peterkofsky
  • P. Suryanarayana Murthy
Publisher
American Society for Microbiology
Publication Date
Sep 01, 2003
Source
PMC
Keywords
Disciplines
  • Biology
License
Unknown

Abstract

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.

Report this publication

Statistics

Seen <100 times