The Journal of General and Applied Microbiology
Online ISSN : 1349-8037
Print ISSN : 0022-1260
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Beauvericin synthetase contains a calmodulin binding motif in the entomopathogenic fungus Beauveria bassiana
Jiyoung KimGi-Ho Sung
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2018 Volume 64 Issue 3 Pages 145-147

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Abstract

Beauvericin is a mycotoxin which has insecticidal, anti-microbial, anti-viral and anti-cancer activities. Beauvericin biosynthesis is rapidly catalyzed by the beauvericin synthetase (BEAS) in Beauveria bassiana. Ca2+ plays crucial roles in multiple signaling pathways in eukaryotic cells. These Ca2+ signals are partially decoded by Ca2+ sensor calmodulin (CaM). In this report, we describe that B. bassiana BEAS (BbBEAS) can interact with CaM in a Ca2+-dependent manner. A synthetic BbBEAS peptide, corresponding to the putative CaM-binding motif, formed a stable complex with CaM in the presence of Ca2+. In addition, in vitro CaM-binding assay revealed that the His-tagged BbBEAS (amino acids 2421–2538) binds to CaM in a Ca2+-dependent manner. Therefore, this work suggests that BbBEAS is a novel CaM-binding protein in B. bassiana.

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© 2018, Applied Microbiology, Molecular and Cellular Biosciences Research Foundation
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