Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

Daniel A. Nissley; Yang Jiang; Fabio Trovato; Ian Sitarik; Karthik B. Narayan; Philip To; Yingzi Xia; Stephen D. Fried; Edward P. O’Brien

doi:10.1038/s41467-022-30548-5

Nature Communications (Jun 2022)

Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional

Daniel A. Nissley,
Yang Jiang,
Fabio Trovato,
Ian Sitarik,
Karthik B. Narayan,
Philip To,
Yingzi Xia,
Stephen D. Fried,
Edward P. O’Brien

Affiliations

Daniel A. Nissley: Department of Chemistry, Pennsylvania State University
Yang Jiang: Department of Chemistry, Pennsylvania State University
Fabio Trovato: Department of Chemistry, Pennsylvania State University
Ian Sitarik: Department of Chemistry, Pennsylvania State University
Karthik B. Narayan: Department of Chemistry, Pennsylvania State University
Philip To: Department of Chemistry, Johns Hopkins University
Yingzi Xia: Department of Chemistry, Johns Hopkins University
Stephen D. Fried: Department of Chemistry, Johns Hopkins University
Edward P. O’Brien: Department of Chemistry, Pennsylvania State University

DOI: https://doi.org/10.1038/s41467-022-30548-5
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 16

Abstract

Read online

Nissley and co-workers predict protein misfolding into kinetically trapped, entangled conformations that can bypass the proteostasis network to remain soluble but less-functional for long timescales is widespread within the E. coli proteome.

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/

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