Identification of calmodulin binding proteins in the entomopathogenic fungus Beauveria bassiana

Calmodulin (CaM) is a primary Ca 2+ 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 C...

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Bibliographic Details
Published in:Folia microbiologica 2018, Vol.63 (1), p.13-16
Main Authors: Kim, Jiyoung, Oh, Junsang, Yoon, Deok-Hyo, Sung, Gi-Ho
Format: Article
Language:English
Subjects:
Applied Microbiology
ATP
Beauveria bassiana
Biomedical and Life Sciences
Calcium
Calcium-binding protein
Calmodulin
Entomopathogenic fungi
Environmental Engineering/Biotechnology
Eukaryotes
Fungi
Heat shock proteins
Hsp70 protein
Immunology
Immunoprecipitation
Life Sciences
Mass spectrometry
Mass spectroscopy
Microbiology
Original Article
Plants (botany)
Proteins
Proteomics
Regulatory mechanisms (biology)
Yeast
Yeasts
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Summary:Calmodulin (CaM) is a primary Ca 2+ 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 ( Bb HSP70) in B. bassiana. Our biochemical study showed that ATP inhibits the molecular interaction between Bb HSP70 and CaM, suggesting a regulatory mechanism between CaM and ATP for regulating Bb HSP70.
ISSN:0015-5632
1874-9356
DOI:10.1007/s12223-017-0529-4