4.7 Article

Distinct phosphorylation and dephosphorylation dynamics of protein arginine kinases revealed by fluorescent activity probes

Journal

CHEMICAL COMMUNICATIONS
Volume 55, Issue 52, Pages 7482-7485

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cc03285a

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Funding

  1. National Research Foundation of Korea [2015R1C1A1A02036405]
  2. POSCO Science Fellowship of POSCO TJ Park Foundation
  3. UNIST [1.150106.01]
  4. 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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