Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis

authored by
Alexander K.W. Elsholz, Kürşad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Abstract

Reversible protein phosphorylation is an important and ubiquitous protein modification in all living cells. Here we report that protein phosphorylation on arginine residues plays a physiologically significant role. We detected 121 arginine phosphorylation sites in 87 proteins in the Gram-positive model organism Bacillus subtilis in vivo. Moreover, we provide evidence that protein arginine phosphorylation has a functional role and is involved in the regulation of many critical cellular processes, such as protein degradation, motility, competence, and stringent and stress responses. Our results suggest that in B. subtilis the combined activity of a protein arginine kinase and phosphatase allows a rapid and reversible regulation of protein activity and that protein arginine phosphorylation can play a physiologically important and regulatory role in bacteria.

Organisation(s)
Institute of Microbiology
External Organisation(s)
University of Greifswald
Freie Universität Berlin
Type
Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Volume
109
Pages
7451-7456
No. of pages
6
ISSN
0027-8424
Publication date
08.05.2012
Publication status
Published
Peer reviewed
Yes
ASJC Scopus subject areas
General
Electronic version(s)
https://doi.org/10.1073/pnas.1117483109 (Access: Open)