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在共伴侣 HSP70/HSP90 组织蛋白 (HOP) 中 ATP 酶活性和 ATP 依赖性构象变化。

ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP).

机构信息

From the Department of Life Science, Faculty and Graduate School of Engineering and Resource Science, Akita University, Akita 010-8502, Japan.

出版信息

J Biol Chem. 2014 Apr 4;289(14):9880-6. doi: 10.1074/jbc.M114.553255. Epub 2014 Feb 17.

DOI:10.1074/jbc.M114.553255
PMID:24535459
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3975032/
Abstract

Co-chaperones help to maintain cellular homeostasis by modulating the activities of molecular chaperones involved in protein quality control. The HSP70/HSP90-organizing protein (HOP) is a co-chaperone that cooperates with HSP70 and HSP90 in catalysis of protein folding and maturation in the cytosol. We show here that HOP has ATP-binding activity comparable to that of HSP70/HSP90, and that HOP slowly hydrolyzes ATP. Analysis of deletion mutants revealed that the ATPase domain of HOP is in the N-terminal TPR1-DP1-TPR2A segment. In addition, HOP changes its conformation in the presence of ATP. These results indicate that HOP is a unique co-chaperone that undergoes an ATP-dependent conformational change.

摘要

伴侣蛋白通过调节参与蛋白质质量控制的分子伴侣的活性来帮助维持细胞内的稳态。HSP70/HSP90 组织蛋白 (HOP) 是一种伴侣蛋白，它与 HSP70 和 HSP90 合作，在细胞质中催化蛋白质折叠和成熟。我们在这里表明，HOP 具有与 HSP70/HSP90 相当的 ATP 结合活性，并且 HOP 缓慢水解 ATP。对缺失突变体的分析表明，HOP 的 ATP 酶结构域位于 N 端 TPR1-DP1-TPR2A 片段中。此外，HOP 在存在 ATP 的情况下改变其构象。这些结果表明，HOP 是一种独特的伴侣蛋白，它经历一个依赖于 ATP 的构象变化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/3796f64e08a6/zbc0181480540006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/ae57694229da/zbc0181480540001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/16ae1508b6a8/zbc0181480540002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/05579cd6384a/zbc0181480540003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/3e44088a2d94/zbc0181480540004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/afc76a078943/zbc0181480540005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/3796f64e08a6/zbc0181480540006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/ae57694229da/zbc0181480540001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/16ae1508b6a8/zbc0181480540002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/05579cd6384a/zbc0181480540003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/3e44088a2d94/zbc0181480540004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/afc76a078943/zbc0181480540005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6ac3/3975032/3796f64e08a6/zbc0181480540006.jpg

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