Evolution of short linear motifs and disordered proteins Topic: yeast as model system to study evolution.

Autor: Sangster AG; Cell & Systems Biology, University of Toronto, 25 Harbord St., Toronto, ON M5S 3G5, Canada., Zarin T; Cell & Systems Biology, University of Toronto, 25 Harbord St., Toronto, ON M5S 3G5, Canada. Electronic address: https://twitter.com/@taraneh_z., Moses AM; Cell & Systems Biology, University of Toronto, 25 Harbord St., Toronto, ON M5S 3G5, Canada. Electronic address: alan.moses@utoronto.ca.
Jazyk: angličtina
Zdroj: Current opinion in genetics & development [Curr Opin Genet Dev] 2022 Oct; Vol. 76, pp. 101964. Date of Electronic Publication: 2022 Aug 05.
DOI: 10.1016/j.gde.2022.101964
Abstrakt: Evolutionary preservation of protein structure had a major influence on the field of molecular evolution: changes in individual amino acids that did not disrupt protein folding would either have no effect or subtly change the 'lock' so that it could fit a new 'key'. Homology of individual amino acids could be confidently assigned through sequence alignments, and models of evolution could be tested. This view of molecular evolution excluded large regions of proteins that could not be confidently aligned, such as intrinsically disordered regions (IDRs) that do not fold into stable structures. In the last decade, major progress has been made in understanding the evolution of IDRs, much of it facilitated by new experimental and computational approaches in yeast. Here, we review this progress as well as several still outstanding questions.
(Copyright © 2022 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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