Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9121658 | FEMS Microbiology Letters | 2005 | 7 Pages |
Abstract
The gene, named cabB, encoding a calmodulin-like protein of 70 amino acids containing two helix-loop-helix EF-hand motifs was cloned from Streptomyces coelicolor A3(2). cabB was transcribed from a single promoter throughout growth. The CabB protein produced in Escherichia coli was a monomer in solution, although it corresponded to one half of a dumbbell shape of the eukaryotic calmodulins. CabB bound calcium and upon binding of calcium its α-helix content was increased, as determined by circular dichroism spectroscopy. The growth of cabB-disruptants (mutant ÎcabB) on minimal agar medium containing calcium higher than 20 mM was delayed, suggesting that CabB has a role in calcium homeostasis by serving as a calcium buffer or transporter, as suggested for calerythrin in actinomycetes and the invertebrate sarcoplasmic calcium-binding proteins. Wide distribution of cabB almost exclusively in actinomycetes suggests a common role of EF-hand CabB-type proteins in these filamentous, soil-dwelling Gram-positive bacterial genera.
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Authors
Tohru Yonekawa, Yasuo Ohnishi, Sueharu Horinouchi,