Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 7451-7456 |
| Seitenumfang | 6 |
| Fachzeitschrift | Proceedings of the National Academy of Sciences of the United States of America |
| Jahrgang | 109 |
| Ausgabenummer | 19 |
| Publikationsstatus | Veröffentlicht - 8 Mai 2012 |
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.
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in: Proceedings of the National Academy of Sciences of the United States of America, Jahrgang 109, Nr. 19, 08.05.2012, S. 7451-7456.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis
AU - Elsholz, Alexander K.W.
AU - Turgay, Kürşad
AU - Michalik, Stephan
AU - Hessling, Bernd
AU - Gronau, Katrin
AU - Oertel, Dan
AU - Mäder, Ulrike
AU - Bernhardt, Jörg
AU - Becher, Dörte
AU - Hecker, Michael
AU - Gerth, Ulf
N1 - Copyright: Copyright 2013 Elsevier B.V., All rights reserved.
PY - 2012/5/8
Y1 - 2012/5/8
N2 - 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.
AB - 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.
KW - ClpC
KW - HSP100/Clp
KW - McsB
KW - Phosphagen kinase
KW - YwlE
UR - http://www.scopus.com/inward/record.url?scp=84860805449&partnerID=8YFLogxK
U2 - 10.1073/pnas.1117483109
DO - 10.1073/pnas.1117483109
M3 - Article
C2 - 22517742
AN - SCOPUS:84860805449
VL - 109
SP - 7451
EP - 7456
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 19
ER -