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Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function

Authors :
Simon Maria Kienle
Tobias Schneider
Katrin Stuber
Christoph Globisch
Jasmin Jansen
Florian Stengel
Christine Peter
Andreas Marx
Michael Kovermann
Martin Scheffner
Source :
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Publication Year :
2022
Publisher :
Nature Portfolio, 2022.

Abstract

Ubiquitin is not only a posttranslational modifier but itself is subject to modifications, such as acetylation. Characterization of distinct acetylated ubiquitin variants reveals that each acetylation site has a particular impact on ubiquitin structure and its protein-protein interaction properties.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
13
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.1e21cc4548474d48816030ee2117176a
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-022-33087-1