About YU

News

Professor KIM Dong-young's research team of YU Department of Pharmacy identified the structure of protein-arginine phosp N

No.10600042
  • Writer PR team
  • Date : 2024.05.09 14:33
  • Publication Date : 2024.04.26
  • Views : 603

Identification of the structure of protein-arginine kinase active complex, for the first time in the world

Published in a renowned international academic journal <Proceedings of the National Academy of Sciences of the United States (PNAS)>

[April 26, 2024]


의류, 사람, 인간의 얼굴, 텍스트이(가) 표시된 사진

자동 생성된 설명

<Professor KIM Dong-young’s research team of YU Department of Pharmacy (from the left, Professor KIM Dong-young and doctoral student Aripuzaman)>


Professor Kim Dong-young's research team of YU Department of Pharmacy (President CHOI Oe-chool) announced that they identified the principle of activation of this enzyme by analyzing the structure and enzyme activity of protein-arginine phosphatase complex.


 Protein plays a very important role in the body. Even after synthesis, the function of protein is controlled with continuous modification. In the process, the most common modification is “phosphorylation.” Phosphorylation means that a phosphate group (PO4) is attached to a protein and, when phosphorylated, the activity and function of protein are controlled and almost all actions in the body including memory and signal transmission are controlled. Usually, phosphorylation of protein aims at the amino acid having a hydroxyl group (-OH) but gram-positive bacteria have an enzyme that phosphorylates arginine in protein. This enzyme is activated in the high-temperature environment, allowing bacteria to control the degradation of intracellular proteins through arginine phosphorylation. It may be said that protein phosphorylation-arginine is a special protein degradation control method in bacteria to correspond to ubiquitin in eukaryotic cells.


 The importance of protein-arginine phosphorylation enzyme in bacterial stress response and protein degradation has been highlighted but it has not been clearly known how the activity of this enzyme is controlled. Therefore, the research team identified the structure of the active complex of protein-arginine phosphorylation enzyme for the first time in the world and showed the principle of activation of this enzyme


Professor KIM Dong-young said, “This study is significant in identifying the structure of protein-arginine phosphatase complex, whose function has not been clearly identified due to the difficulty in the experimental process and is an important clue to understand the stress response of bacteria.”


 Meanwhile, this study was led by Professor KWON Eun-ju of Gyeongsang National University and doctoral student Aripuzaman of the Graduate School of Pharmacy and the research results were published in Proceedings of the National Academy of Sciences (PNAS) on April 23.