Identification of calmodulin binding proteins in the entomopathogenic fungus Beauveria bassiana

. 2018 Jan ; 63 (1) : 13-16. [epub] 20170511

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid28497337

Grantová podpora
PJ011949 Rural Development Administration, Korea

Odkazy

PubMed 28497337
DOI 10.1007/s12223-017-0529-4
PII: 10.1007/s12223-017-0529-4
Knihovny.cz E-zdroje

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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Secretomic analysis of Beauveria bassiana related to cattle tick, Rhipicephalus microplus, infection

. 2019 May ; 64 (3) : 361-372. [epub] 20181025

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