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首页> 美国卫生研究院文献>other >Specific binding of tetratricopeptide repeat (TPR) proteins to heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) is regulated by affinity and phosphorylation
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Specific binding of tetratricopeptide repeat (TPR) proteins to heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) is regulated by affinity and phosphorylation

机译：四肽重复序列（TPR）蛋白与热休克蛋白70（Hsp70）和热休克蛋白90（Hsp90）的特异性结合通过亲和力和磷酸化来调节

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摘要

The heat shock proteins Hsp70 and Hsp90 require the help of tetratricopeptide repeat (TPR) domain-containing co-chaperones for many of their functions. Each monomer of Hsp70 or Hsp90 can only interact with a single TPR co-chaperone at a time and each member of the TPR co-chaperone family brings distinct functions into the complex. Thus, competition for TPR binding sites on Hsp70 and Hsp90 appears to shape chaperone activity. Recent structural and biophysical efforts have improved our understanding of chaperone-TPR contacts, focusing on the C-terminal EEVD motif that is present in both chaperones. To better understand these important protein-protein interactions on a wider scale, we measured the affinity of five TPR co-chaperones, CHIP, Hop, DnaJC7, FKBP51, and FKBP52, for the C-termini of four members of the chaperone family, Hsc70, Hsp72, Hsp90α, and Hsp90β, in vitro. These studies identified some surprising selectivity amongst the chaperone-TPR pairs, including the selective binding of FKBP51/52 to Hsp90α/β. These results also revealed that other TPR co-chaperones are only able to weakly discriminate between the chaperones or between their paralogs. We also explored whether mimicking phosphorylation of serine and threonine residues near the EEVD motif might impact affinity and found that pseudophosphorylation had selective effects on binding to CHIP but not other co-chaperones. Together, these findings suggest that both intrinsic affinity and post-translational modifications tune the interactions between Hsp70/90 and the TPR co-chaperones.
机译：热休克蛋白Hsp70和Hsp90需要具有四三肽重复（TPR）结构域的伴侣分子的帮助才能发挥其许多功能。 Hsp70或Hsp90的每个单体一次只能与一个TPR伴侣分子相互作用，而TPR伴侣分子家族的每个成员都将不同的功能带入复合物中。因此，对Hsp70和Hsp90上TPR结合位点的竞争似乎可以塑造伴侣活性。最近的结构和生物物理学方面的努力提高了我们对分子伴侣-TPR接触的理解，重点是两种分子伴侣中均存在C端EEVD基序。为了更广泛地了解这些重要的蛋白质-蛋白质相互作用，我们测量了五个TPR伴侣分子CHIP，Hop，DnaJC7，FKBP51和FKBP52对伴侣分子家族四个成员Hsc70的C末端的亲和力。 ，Hsp72，Hsp90α和Hsp90β在体外。这些研究在伴侣-TPR对中发现了一些令人惊讶的选择性，包​​括FKBP51 / 52与Hsp90α/β的选择性结合。这些结果还表明，其他TPR辅助伴侣分子仅能微弱地区分伴侣分子或其旁系同源物。我们还探讨了模仿EEVD基序附近的丝氨酸和苏氨酸残基的磷酸化是否会影响亲和力，并发现伪磷酸化对CHIP的结合具有选择性作用，但对其他伴侣分子则没有影响。总之，这些发现表明内在亲和力和翻译后修饰均可调节Hsp70 / 90与TPR伴侣分子之间的相互作用。

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