Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast

Guanidine hydrochloride reactivates an ancient septin hetero-oligomer assembly pathway in budding yeast

Septin proteins evolved from ancestral GTPases and co-assemble into hetero-oligomers and cytoskeletal filaments. In Saccharomyces cerevisiae, five septins comprise two species of hetero-octamers, Cdc11/Shs1–Cdc12–Cdc3–Cdc10–Cdc10–Cdc3–Cdc12–Cdc11/Shs1. Slow GTPase activity by Cdc12 directs the choic...

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Bibliographic Details
Main Authors: Courtney R Johnson, Marc G Steingesser, Andrew D Weems, Anum Khan, Amy Gladfelter, Aurélie Bertin, Michael A McMurray
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2020-01-01
Series:eLife
Subjects:
septins
oligomerization
protein folding
guanidine
chaperone
Online Access:https://elifesciences.org/articles/54355

Internet

https://elifesciences.org/articles/54355

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