Kim Jiyoung, Oh Junsang, Yoon Deok-Hyo, Sung Gi-Ho
Institute for Bio-Medical Convergence, International St. Mary's Hospital and College of Medicine, Catholic Kwandong University, Incheon, 404-834, South Korea.
College of Pharmacy, Chung-Ang University, Seoul, South Korea.
Folia Microbiol (Praha). 2018 Jan;63(1):13-16. doi: 10.1007/s12223-017-0529-4. Epub 2017 May 11.
Calmodulin (CaM) is a primary Ca 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.
钙调蛋白（CaM）是一种主要的钙受体，在真核生物的多种细胞反应中起关键作用。尽管在酵母、植物和动物中大量的钙调蛋白结合蛋白已为人所知，但关于丝状真菌中钙调蛋白靶向蛋白却知之甚少。为了鉴定丝状真菌中的钙调蛋白结合蛋白，我们在球孢白僵菌中使用了一种蛋白质组学方法，结合免疫共沉淀（CoIP）和基质辅助激光解吸电离飞行时间串联质谱（MALDI-TOF/TOF MS）。通过这种方法，我们在球孢白僵菌中鉴定出了10种钙调蛋白结合蛋白。其中一种钙调蛋白靶向蛋白是球孢白僵菌中的热休克蛋白70（BbHSP70）。我们的生化研究表明，ATP抑制BbHSP70与CaM之间的分子相互作用，这表明CaM与ATP之间存在一种调节BbHSP70的调控机制。
