摘要 Molecular chaperones, also known as heat shock 蛋白

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論文資訊

• 類型：已發表論文
• 日期：2016

摘要

Molecular chaperones, also known as heat-shock 蛋白質s, refold misfolded 蛋白質s and help other 蛋白質s reach their native conformation. Thanks to these abilities, some chaperones, such as the Hsp90 蛋白質 or the chaperonin GroEL, can buffer the deleterious phenotypic effects of 突變s that alter 蛋白質 structure and function. Hsp70 chaperones use a chaperoning mechanism different from that of Hsp90 and GroEL, and it is not known whether they can also buffer 突變s. Here, we show that they can. To this end, we performed a 突變 accumulation experiment in Escherichia coli, followed by whole-基因組 resequencing. Overexpression of the Hsp70 chaperone DnaK helps cells cope with 突變al load and completely avoid the extinctions we observe in lineages evolving without chaperone overproduction. Additionally, our sequence data

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