Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria.
Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria.
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DOI：
10.1007/s12192-010-0233-7
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发表时间：
2011-03
影响因子：
3.8
通讯作者：
Cid C
中科院分区：
文献类型：
--
作者：
García-Descalzo L;Alcazar A;Baquero F;Cid C
热休克蛋白 90 (HSP90) 是一种保守的分子伴侣，作为复合物的一部分发挥作用，其中不同的客户蛋白将其靶向不同的底物组。在本文中，研究人员在温和环境（Shewanella oneidensis）和寒冷环境（Shewanella frigidimarina 和 Psychrobacter frigidicola）的 γ-变形菌中研究了 HSP90 复合物，以确定 HSP90 与客户蛋白相互作用因适应寒冷环境而发生的变化。使用特异性抑制剂 17-烯丙氨基-格尔德霉素测定 HSP90 参与冷适应的情况。然后，从细菌培养物中免疫沉淀HSP90，通过二维凝胶电泳分析HSP90复合物中的蛋白质，并通过基质辅助激光解吸/电离飞行时间质谱法进行鉴定。根据 HSP90 相关蛋白分析，在同一属 S. oneidensis 和 S. frigidimarina 的两个物种中仅发现了 15 种常见蛋白，而在嗜冷物种 S. frigidimarina 和 P. frigidimarina 21 中发现的常见蛋白数量显着增加 (p<0.001)。这三个物种中只有两种 HSP90 相互作用蛋白是共有的，即伴侣蛋白 DnaK 和 GroEL。有趣的是，一些与能量代谢相关的蛋白质（异柠檬酸裂解酶、琥珀酰辅酶A合成酶、乙醇脱氢酶、NAD（+）合酶和苹果酸脱氢酶）和一些翻译因子仅与嗜冷细菌中的HSP90相互作用。我们可以得出结论，HSP90和HSP90相关蛋白可能参与了适应寒冷环境的机制，有趣的是，生活在相似环境中的生物体与来自不同环境的同属但系统发育密切相关的生物体保存了相似的潜在HSP90相互作用子。
Heat shock protein 90 (HSP90) is a conserved molecular chaperone that functions as part of complexes in which different client proteins target it to diverse sets of substrates. In this paper, HSP90 complexes were investigated in γ-proteobacteria from mild (Shewanella oneidensis) and cold environments (Shewanella frigidimarina and Psychrobacter frigidicola), to determine changes in HSP90 interactions with client proteins in response to the adaptation to cold environments. HSP90 participation in cold adaptation was determined using the specific inhibitor 17-allylamino-geldanamycin. Then, HSP90 was immunoprecipitated from bacterial cultures, and the proteins in HSP90 complexes were analyzed by two-dimensional gel electrophoresis and identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. According to HSP90-associated protein analysis, only 15 common proteins were found in both species from the same genus, S. oneidensis and S. frigidimarina, whereas a significant higher number of common proteins were found in both psychrophilic species S. frigidimarina and P. frigidicola 21 (p < 0.001). Only two HSP90-interacting proteins, the chaperone proteins DnaK and GroEL, were common to the three species. Interestingly, some proteins related to energy metabolism (isocitrate lyase, succinyl-CoA synthetase, alcohol dehydrogenase, NAD(+) synthase, and malate dehydrogenase) and some translation factors only interacted with HSP90 in psychrophilic bacteria. We can conclude that HSP90 and HSP90-associated proteins might take part in the mechanism of adaptation to cold environments, and interestingly, organisms living in similar environments conserve similar potential HSP90 interactors in opposition to phylogenetically closely related organisms of the same genus but from different environments.