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首页> 外文期刊>Journal of Molecular Biology >An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function.
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An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function.

机译：Hsp90伴侣蛋白p23的无结构C末端区域对其伴侣功能很重要。

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摘要

p23 is a co-chaperone of the heat shock protein Hsp90. p23 binds to Hsp90 in its ATP-bound state and, on its own, interacts specifically with non-native proteins. In our attempt to correlate these functions to specific regions of p23 we have identified an unstructured region in p23 that maps to the C-terminal part of the protein sequence. This unstructured region is dispensible for interaction of p23 with Hsp90, since truncated p23 can still form complexes with Hsp90. In contrast, however, truncation of the C-terminal 30 amino acid residues of p23 affects the ability of p23 to bind non-native proteins and to prevent their non-specific aggregation. The isolated C-terminal region itself is not able to act as a chaperone nor is it possible to complement truncated p23 by addition of this peptide. These results imply that the binding site for Hsp90 is contained in the folded domain of p23 and that for efficient interaction of p23 with non-native proteins both the folded domain and the C-terminal unstructured region are required. Copyright 1999 Academic Press.
机译：p23是热激蛋白Hsp90的伴侣蛋白。 p23以其ATP结合状态与Hsp90结合，并独自与非天然蛋白特异性相互作用。在我们试图将这些功能与p23的特定区域相关联的过程中，我们确定了p23中一个非结构化区域，该区域映射到蛋白质序列的C末端。该非结构化区域对于p23与Hsp90的相互作用是必不可少的，因为截短的p23仍然可以与Hsp90形成复合物。相反，p23的C端30个氨基酸残基被截断会影响p23结合非天然蛋白并阻止其非特异性聚集的能力。分离的C末端区域本身不能充当伴侣分子，也不可能通过添加该肽来补充截短的p23。这些结果暗示Hsp90的结合位点包含在p23的折叠结构域中，并且为了使p23与非天然蛋白有效相互作用，需要折叠结构域和C末端非结构化区域。版权所有1999，学术出版社。

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