Chaperone-client interactions: Non-specificity engenders multifunctionality

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Chaperone-client interactions: Non-specificity engenders multifunctionality.

Here, we provide an overview of the different mechanisms whereby three different chaperones, Spy, Hsp70, and Hsp60, interact with folding proteins, and we discuss how these chaperones may guide the folding process. Available evidence suggests that even a single chaperone can use many mechanisms to aid in protein folding, most likely due to the need for most chaperones to bind clients promiscuou...

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A molecular mechanism of chaperone-client recognition

Molecular chaperones are essential in aiding client proteins to fold into their native structure and in maintaining cellular protein homeostasis. However, mechanistic aspects of chaperone function are still not well understood at the atomic level. We use nuclear magnetic resonance spectroscopy to elucidate the mechanism underlying client recognition by the adenosine triphosphate-independent cha...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2017

ISSN: 0021-9258

DOI: 10.1074/jbc.r117.796862