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原文連結
論文資訊
- 類型：已發表論文
- 日期：2014-09-21
摘要
Heat-shock 蛋白質 90 (Hsp90) promotes the maturation and stability of its client 蛋白質s, including many kinases. In doing so, Hsp90may allow its clients to accumulate突變s as previously proposed by the capacitor hypothesis. If true, Hsp90 clients should show increased 演化ary rate compared with nonclients; however, other factors, such as gene expression and 蛋白質 connectivity, may confound or obscure the chaperone's putative contribution. Here, we compared the 演化ary rates of many Hsp90 clients and nonclients in the human 蛋白質 kinase superfamily. We show that Hsp90 client status promotes 演化ary rate independently of, but in a small magnitude similar to that of gene expression and 蛋白質 connectivity. Hsp90's effect on kinase 演化ary rate was detected acrossmammals, specifically relaxing purifying selection.
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