Open AccessPresence of calmodulin‐like calcium‐binding protein in Bacillus cereus T spores
Author(s) -
Shyu Yuantay,
Foegeding Peggy M.
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03117.x
Subject(s) - calmodulin , bacillus cereus , calcium , spore , cereus , biochemistry , chemistry , sepharose , affinity chromatography , binding protein , calcium binding protein , chromatography , biology , bacteria , microbiology and biotechnology , enzyme , organic chemistry , gene , genetics
Bacillus cereus T spores were extensively washed, broken, and heated at 90°C for 2 min. Using calcium‐dependent hydrophobic interaction chromatography, a single peak protein fraction was obtained which possessed calcium‐binding capacity and some characteristics of calmodulin. This heat‐stable protein fraction was retained by hydrophobic matrices (Phenyl‐Sepharose) or a calmodulin antagonist (naphthalenesulfonamide) in a calcium‐dependent manner. Calcium binding ability was verified by 45 Ca autoradiography and a competitive calcium binding assay using Chelex‐100. The crude spore extract displaced bovine brain calmodulin from its antibody in a radioimmunoassay and the immunoreactive specific activity of the partially purified fraction was approx. 200‐fold greater than the crude spore extract. Thus, B. cereus T spores have a calcium‐binding protein with calmodulin‐like properties.