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)
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)