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A novel chlorination-induced ribonuclease YabJ from
Hyo Jung Kim1, Ae-Ran Kwon2, Bong-Jin Lee3
1Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-gu, Seoul 151-742, Korea.
Bioscience Reports
|September 12, 2018
Summary
Chlorination of the bacterial protein YabJ, a RidA homolog, does not induce chaperone activity but instead activates ribonuclease function. This finding reveals a new role for chlorination as a post-translational modification in bacteria.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Protein structure dictates biological function, but post-translational modifications (PTMs) like chlorination can alter protein activity.
- The importance of chlorination as a PTM is not well understood, with limited studies available.
- While some bacterial RidA proteins exhibit chaperone activity after chlorination, this function is not universally observed across the family.
Purpose of the Study:
- To investigate the structural and functional changes in a Staphylococcus aureus RidA homolog, YabJ, upon chlorination.
- To determine if chlorination induces chaperone activity in S. aureus YabJ, contrasting with findings in E. coli RidA.
- To explore potential novel functions of YabJ related to chlorination.
Main Methods:
- Structural analysis of S. aureus YabJ, comparing it to other YjgF family members.
- Biochemical assays to assess YabJ activity, including chaperone and ribonuclease functions, before and after chlorination.
- Investigating the stability and reversibility of chlorinated YabJ using DTT treatment.
Main Results:
- S. aureus YabJ shares structural similarities with other YjgF family proteins, featuring conserved surface pockets.
- Chlorination enhances the stability of YabJ, and this modification is reversible.
- Unlike E. coli RidA, S. aureus YabJ does not gain chaperone activity after chlorination.
- Chlorination induces significant ribonuclease activity in YabJ, which decreases upon reduction.
- This is the first identification of nucleic acid-related activity for bacterial RidA family proteins.
Conclusions:
- S. aureus YabJ functions as a novel chlorination-activated ribonuclease, a previously unidentified activity for the bacterial RidA family.
- Chlorination acts as a PTM that switches YabJ function from a potentially structural role to enzymatic activity.
- This study expands the understanding of chlorination's impact on protein function and highlights a new PTM mechanism in bacteria.
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