Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine

Hisham Mazal; Marija Iljina; Yoav Barak; Nadav Elad; Rina Rosenzweig; Pierre Goloubinoff; Inbal Riven; Gilad Haran

doi:10.1038/s41467-019-09474-6

Nature Communications (Mar 2019)

Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine

Hisham Mazal,
Marija Iljina,
Yoav Barak,
Nadav Elad,
Rina Rosenzweig,
Pierre Goloubinoff,
Inbal Riven,
Gilad Haran

Affiliations

Hisham Mazal: Department of Chemical and Biological Physics, Weizmann Institute of Science
Marija Iljina: Department of Chemical and Biological Physics, Weizmann Institute of Science
Yoav Barak: Department of Chemical Research Support, Weizmann Institute of Science
Nadav Elad: Department of Chemical Research Support, Weizmann Institute of Science
Rina Rosenzweig: Department of Structural Biology, Weizmann Institute of Science
Pierre Goloubinoff: Department of Plant Molecular Biology, Faculty of Biology and Medicine, University of Lausanne
Inbal Riven: Department of Chemical and Biological Physics, Weizmann Institute of Science
Gilad Haran: Department of Chemical and Biological Physics, Weizmann Institute of Science

DOI: https://doi.org/10.1038/s41467-019-09474-6
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 12

Abstract

Read online

Large protein machines are tightly regulated through allosteric communication channels. Here authors use single-molecule FRET and demonstrate the involvement of ultrafast conformational dynamics in the allosteric regulation of ClpB, a hexameric AAA+ machine that rescues aggregated proteins.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal