Identification of calmodulin binding proteins in the entomopathogenic fungus Beauveria bassiana
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
Grantová podpora
PJ011949
Rural Development Administration, Korea
PubMed
28497337
DOI
10.1007/s12223-017-0529-4
PII: 10.1007/s12223-017-0529-4
Knihovny.cz E-zdroje
- MeSH
- adenosintrifosfát metabolismus MeSH
- Beauveria chemie genetika metabolismus MeSH
- fungální proteiny chemie genetika metabolismus MeSH
- hmyz mikrobiologie MeSH
- kalmodulin chemie genetika metabolismus MeSH
- proteiny vázající kalmodulin chemie genetika metabolismus MeSH
- proteomika MeSH
- sekvence aminokyselin MeSH
- sekvenční seřazení MeSH
- tandemová hmotnostní spektrometrie MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- adenosintrifosfát MeSH
- fungální proteiny MeSH
- kalmodulin MeSH
- proteiny vázající kalmodulin MeSH
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.
Zobrazit více v PubMed
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