Identification of calmodulin binding proteins in the entomopathogenic fungus Beauveria bassiana

Folia Microbiologica
Jiyoung KimGi-Ho Sung

Abstract

Calmodulin (CaM) is a primary Ca2+ receptor and plays a pivotal role in a variety of cellular responses in eukaryotes. Even though a large number of CaM-binding proteins are well known in yeast, plants, and animals, little is known regarding CaM-targeted proteins in filamentous fungi. To identify CaM-binding proteins in filamentous fungi, we used a proteomics method coupled with co-immunoprecipitation (CoIP) and MALDI-TOF/TOF mass spectrometry (MS) in Beauveria bassiana. Through this method, we identified ten CaM-binding proteins in B. bassiana. One of the CaM-targeted proteins was the heat shock protein 70 (BbHSP70) in B. bassiana. Our biochemical study showed that ATP inhibits the molecular interaction between BbHSP70 and CaM, suggesting a regulatory mechanism between CaM and ATP for regulating BbHSP70.

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Jul 17, 2016·Biochimica Et Biophysica Acta·Jiyoung KimGi-Ho Sung

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Citations

Oct 27, 2018·Folia Microbiologica·Lucélia SantiWalter O Beys-da-Silva

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Datasets Mentioned

BETA
AAX43782

Methods Mentioned

BETA
protein folding

Software Mentioned

MASCOT
Model
Swiss

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