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

Hoyoung Jung1, Yigun Choi1, Donghee Lee1

  • 1Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea. jmkee@unist.ac.kr.

Chemical Communications (Cambridge, England)
|June 12, 2019
PubMed

Insights

Bacterial protein arginine phosphorylation is regulated by the McsB kinase. This kinase can dephosphorylate phosphoarginine (pArg) residues, producing ATP from ADP, and dynamically control pArg levels without a phosphatase.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Protein arginine phosphorylation is a key regulatory mechanism in bacterial stress responses and virulence.
  • The role of specific kinases in controlling these phosphorylation events is crucial for understanding bacterial adaptation.

Purpose of the Study:

  • To investigate the enzymatic activity of the bacterial protein arginine kinase McsB.
  • To elucidate the mechanism by which McsB regulates protein arginine phosphorylation levels.
  • To explore the potential of McsB in ATP production.

Main Methods:

  • Utilized fluorescent activity probes to monitor protein arginine phosphorylation.
  • Assayed the dephosphorylation activity of purified McsB protein.
  • Quantified ATP production from ADP in the presence of McsB and phosphoarginine residues.

Main Results:

  • Demonstrated that McsB functions as a protein arginine kinase.
  • Showed that McsB can dephosphorylate phosphoarginine (pArg) residues.
  • Confirmed that McsB catalyzes the production of ATP from ADP during dephosphorylation.
  • Implicated McsB in the dynamic control of protein pArg levels, independent of phosphatase activity.

Conclusions:

  • McsB possesses a unique dual function, acting as a kinase and contributing to energy metabolism.
  • The kinase activity of McsB allows for dynamic regulation of protein arginine phosphorylation.
  • This finding reveals a novel mechanism for controlling bacterial phosphoproteomes and energy levels.

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