Journal
CHEMICAL COMMUNICATIONS
Volume 55, Issue 52, Pages 7482-7485Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cc03285a
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Funding
- National Research Foundation of Korea [2015R1C1A1A02036405]
- POSCO Science Fellowship of POSCO TJ Park Foundation
- UNIST [1.150106.01]
- National Research Foundation of Korea [2015R1C1A1A02036405] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Protein arginine (Arg) phosphorylation regulates stress responses and virulence in bacteria. With fluorescent activity probes, we show that McsB, a protein Arg kinase, can dephosphorylate phosphoarginine (pArg) residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase.
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