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

Autor:	Jung H; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea. jmkee@unist.ac.kr., Choi Y; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea. jmkee@unist.ac.kr., Lee D; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea. jmkee@unist.ac.kr., Seo JK; UNIST Central Research Facilities (UCRF), Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea., Kee JM; Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea. jmkee@unist.ac.kr.
Jazyk:	angličtina
Zdroj:	Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2019 Jul 04; Vol. 55 (52), pp. 7482-7485. Date of Electronic Publication: 2019 Jun 11.
DOI:	10.1039/c9cc03285a
Abstrakt:	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.
Databáze:	MEDLINE
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