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

verfasst von

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.

Organisationseinheit(en)

Institut für Mikrobiologie

Externe Organisation(en)

Ernst-Moritz-Arndt-Universität Greifswald
Freie Universität Berlin (FU Berlin)

Typ

Artikel

Journal

Proceedings of the National Academy of Sciences of the United States of America

Band

109

Seiten

7451-7456

Anzahl der Seiten

6

ISSN

0027-8424

Publikationsdatum

08.05.2012

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Allgemein

Elektronische Version(en)

https://doi.org/10.1073/pnas.1117483109 (Zugang: Offen)