Issue 52, 2019
From the journal:

Chemical Communications

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

Hoyoung Jung,a   Yigun Choi,a   Donghee Lee,a   Jeong Kon Seob  and  Jung-Min Kee ORCID logo *a  

* Corresponding authors

a Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea
E-mail: jmkee@unist.ac.kr

b UNIST Central Research Facilities (UCRF), Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea

Abstract

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.

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

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Article information

DOI
https://doi.org/10.1039/C9CC03285A
Article type
Communication
Submitted
28 Apr 2019
Accepted
03 Jun 2019
First published
04 Jun 2019

Chem. Commun., 2019,55, 7482-7485

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

H. Jung, Y. Choi, D. Lee, J. K. Seo and J. Kee, Chem. Commun., 2019, 55, 7482 DOI: 10.1039/C9CC03285A

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