Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thaliana.
Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thaliana.
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DOI：
10.1534/g3.117.042291
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发表时间：
2017-06-07
期刊：
影响因子：
--
通讯作者：
Sahi C
中科院分区：
文献类型：
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作者：
Verma AK;Diwan D;Raut S;Dobriyal N;Brown RE;Gowda V;Hines JK;Sahi C
70 kDa的热休克蛋白（Hsp70）与结构多样的热休克蛋白40（J蛋白）合作，在各种细胞隔室中产生不同的分子伴侣网络，在所有生物体中执行无数的管家和应激相关功能。植物是无柄的，需要不断地维持其细胞的蛋白质稳态以响应外部环境的提示。在这些情况下，Hsp70：J蛋白机器可能在微调细胞蛋白质质量控制中发挥重要作用。虽然普遍存在，但植物Hsp70：J蛋白网络的功能特异性和复杂性尚未得到研究。在这里，我们分析了拟南芥胞质溶胶中的J蛋白网络，并使用酵母遗传学，表明大多数植物J蛋白在基本伴侣功能中的功能特异性在很长的进化时间尺度上是保守的。详细的系统发育和功能分析表明，增加的数量，监管的差异，并在J蛋白的新功能化共同有助于在高等植物中的热休克蛋白70：J蛋白网络的新兴功能多样性和复杂性。基于所提供的数据，我们提出，高等植物已经编排了他们的“伴侣”，特别是他们的J蛋白补体，根据他们的专门的细胞和生理规定。
Heat shock proteins of 70 kDa (Hsp70s) partner with structurally diverse Hsp40s (J proteins), generating distinct chaperone networks in various cellular compartments that perform myriad housekeeping and stress-associated functions in all organisms. Plants, being sessile, need to constantly maintain their cellular proteostasis in response to external environmental cues. In these situations, the Hsp70:J protein machines may play an important role in fine-tuning cellular protein quality control. Although ubiquitous, the functional specificity and complexity of the plant Hsp70:J protein network has not been studied. Here, we analyzed the J protein network in the cytosol of Arabidopsis thaliana and, using yeast genetics, show that the functional specificities of most plant J proteins in fundamental chaperone functions are conserved across long evolutionary timescales. Detailed phylogenetic and functional analysis revealed that increased number, regulatory differences, and neofunctionalization in J proteins together contribute to the emerging functional diversity and complexity in the Hsp70:J protein network in higher plants. Based on the data presented, we propose that higher plants have orchestrated their “chaperome,” especially their J protein complement, according to their specialized cellular and physiological stipulations.