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Identification of calmodulin binding proteins in the entomopathogenic fungus Beauveria bassiana.

Authors :
Kim J
Oh J
Yoon DH
Sung GH
Source :
Folia microbiologica [Folia Microbiol (Praha)] 2018 Jan; Vol. 63 (1), pp. 13-16. Date of Electronic Publication: 2017 May 11.
Publication Year :
2018

Abstract

Calmodulin (CaM) is a primary Ca <superscript>2+</superscript> 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.

Details

Language :
English
ISSN :
1874-9356
Volume :
63
Issue :
1
Database :
MEDLINE
Journal :
Folia microbiologica
Publication Type :
Academic Journal
Accession number :
28497337
Full Text :
https://doi.org/10.1007/s12223-017-0529-4