Comparison of characterization among Bordetella calmodulin-like protein, bovine brain calmodulin and Escherichia coli acyl-carrier protein.
We previously reported that Bordetella calmodulin-like protein (CLP), like bovine brain calmodulin (CaM), enhances adenylate cyclase and phosphodiesterase activities. In this communication, antigenic and biochemical characters were compared between CLP and CaM. It was found that anti-CLP and anti-CaM sera obtained reacted with CaM and CLP, respectively. The amino acid composition of CLP was similar to CaM. The similarity was also found in an Escherichia coli acyl-carrier protein (ACP), a Ca(2+)-binding protein. Though the amino acid sequence of N-terminus region of CLP has no significant homology with CaM, ACP has highly homology in its N-terminus similar to CaM. These results suggest that CLP might act as a Ca(2+)-binding protein, and/or an ACP during the activation of adenylate cyclase and phosphodiesterase.
Nagai
M
M
Department of Microbiology, School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
Watanabe
M
M
Endoh
M
M
Danbara
H
H
D000213:Acyl Carrier Protein / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry*; D001884:Bordetella / Q000737:chemistry*; D001923:Brain Chemistry / Q000502:physiology; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002147:Calmodulin; D002417:Cattle; D004926:Escherichia coli / Q000737:chemistry*; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D009419:Nerve Tissue Proteins