Behind closed gates – chaperones and charged residues determine protein fate
- 30 April 2020
- journal article
- editorial
- Published by Springer Science and Business Media LLC in The EMBO Journal
- Vol. 39 (11), e104939
- https://doi.org/10.15252/embj.2020104939
Abstract
Charged residues flanking aggregation‐prone regions play a role in protein folding and prevention of aggregation. In this issue of The EMBO Journal, Houben et al exploit the role of such charged gatekeepers in aggregation suppression and find that negative charges are more effective than positive ones. Strikingly, the prominent Hsp70 chaperone has a strong preference for the less effective, basic gate keepers. This implies co‐adaptation of chaperone specificity and composition of protein sequences in evolution.Keywords
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