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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
Published on: August 7, 2021
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A flexible cofactor-binding loop in the novel arginine methyltransferase Sfm1
Caiyan Wang1,2, Jianhua Zeng1,2, Wei Xie1,2
1Key Laboratory of Gene Engineering of the Ministry of Education, State Key Laboratory for Biocontrol, School of Life Sciences, The Sun Yat-Sen University, Guangzhou, China.
FEBS Letters
|December 20, 2016
Summary
Sfm1, an arginine methyltransferase, utilizes a unique SAM-binding loop for ribosomal protein methylation. Structural insights reveal its distinct substrate specificity compared to related enzymes.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Arginine methylation is a crucial post-translational modification impacting cellular functions.
- Sfm1, a novel methyltransferase with a SPOUT domain, targets ribosomal proteins, unlike related RNA methyltransferases.
Discussion:
- Cocrystal structures reveal Sfm1's SAM-binding loop adopts an unusual conformation, influencing cofactor binding.
- The identified SAM double conformations and loop's role in SAM affinity are key findings.
Key Insights:
- Structural analysis elucidates Sfm1's distinct substrate recognition mechanism compared to Trm10.
- This work provides molecular insights into Sfm1's function in arginine methylation.
Outlook:
- Further research can explore the functional implications of Sfm1's unique structural features.
- Understanding Sfm1's mechanism may reveal new therapeutic targets for diseases involving protein methylation.
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