Jung, Che-Hun > Faculty

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RESEARCH

RESEARCH

RESEARCH

RESEARCH
Faculty

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Jung, Che-Hun
Department Chemistry
Major Field of Research enzymology, regulation of metabolic pathways
E-mail jungch@jnu.ac.kr
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Research interests

Che-Hun Jung’s lab studies regulation of proteins and metabolic pathways in E. coli and mammals.

 

1. ppGpp-binding proteins

- ppGpp serves as an alarmone in stringent responses in various microbes. ppGpp regulates replication, transcription, translation and metabolic pathways.

- ppGpp-immobilized columns were constructed and ppGpp-binding proteins were isolated by affinity chromatography. The ppGpp-binding proteins were identified by a mass spectroscopy.

- A method to determine the binding affinity of ppGpp to proteins was developed.

- Studies on the effect of ppGpp binding to various proteins such as cyclic AMP receptor proteins (CRP), histone-like nucleoid structuring protein (H-NS), stringent starvation protein A (SspA), HU alpha (HupA) and proteases are currently undergoing.

 

2. Proteins regulated by ascorbic acid

- Only a few proteins are reported as regulated by ascorbic acid.

- A group of proteins, potentially regulated by ascorbic acid, have been isolated and identified by proteomics approaches.

- Studies on the effect of ascorbic acid to various enzymes are underway.

 

3. Glutathione-binding proteins

- Glutathione (GSH) is the most abundant non-protein thiol in cells. The concentration of GSH has been reported as 17 mM in E. coli when it is grown in glucose-rich media.

- For those ligands with high cellular concentrations such as GSH, the dissociation constant of 0.5 mM (about 3 % of the cellular GSH concentration) will be sufficient for occupying all of the binding sites. A method to measure the weak bindings has been developed and the binding affinities of GSH to various proteins have been reported.

- Studies of the affect of GSH binding to proteins are currently performed.

 

4. DNA-binding proteins

- Many DNA-binding proteins, which regulate gene expression, have been reported.

- A method to quantitate the binding affinity of proteins to DNA has been developed.

- The binding specificity determined by this study may be useful for elucidating the physiological roles of the DNA-binding proteins.

 

 

<그림 최대 3(각 파일 사이즈 1M 이상)>

 

Binding of ppGpp to CRP and H-NS

 

그림입니다.

원본 그림의 이름: CLP000043801408.bmp

원본 그림의 크기: 가로 562pixel, 세로 295pixel

 

 

 

 

 

 

 

Publication

  • 최근 5년간 대표 논문
  • Duysak T, Afzal AR, Jung CH Determination of glutathione-binding to proteins by fluorescence spectroscopy.
  • Biochem Biophys Res Commun. 2021 Jun;557:329-333.
  • Duysak T, Nguyen LP, Jung CH Binding of Glutathione and ppGpp to Stringent Starvation Protein A (SspA) Bull. Kor. Chem. Soc. 2020 Sep;41(9):925-929
  • Hoang HG, Tran TT, Jung CH The Activation of Glycerol Dehydrogenase from Escherichia coli by ppGpp. Bull. Kor. Chem. Soc. 2020 Feb;41(2):133-138.
  • Nguyen TD, Jeong K, Ryu J, Jung CH A rapid screening of ligand binding by measuring intrinsic fluorescence changes of proteins. Bull. Kor. Chem. Soc. 2017 Sep;38(9):1028-1032