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Identification of calmodulin binding proteins in the entomopathogenic fungus Beauveria bassiana
J. Kim, J. Oh, DH. Yoon, GH. Sung,
Language English Country United States
Document type Journal Article
- MeSH
- Adenosine Triphosphate metabolism MeSH
- Beauveria chemistry genetics metabolism MeSH
- Fungal Proteins chemistry genetics metabolism MeSH
- Insecta microbiology MeSH
- Calmodulin chemistry genetics metabolism MeSH
- Calmodulin-Binding Proteins chemistry genetics metabolism MeSH
- Proteomics MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Tandem Mass Spectrometry MeSH
- Protein Binding MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article 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.
References provided by Crossref.org
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- $a 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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