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Toward Understanding Molecular Recognition between PRMTs and their Substrates.

Owen M Price1, Joan M Hevel1

  • 1Department of Chemistry and Biochemistry, Utah State University, Logan, UT 84322, United States.

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|January 25, 2020
PubMed
Summary

Protein arginine methylation is a key process in eukaryotes. This review explores how protein arginine methyltransferases (PRMTs) identify their targets using structural biology, proteomics, and other advanced methods.

Keywords:
PRMTPRMT molecular recognitionarginine methylationarginine methylomesubstrate specificitytarget recognition

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Posttranslational Modifications

Background:

  • Protein arginine methylation is a frequent eukaryotic posttranslational modification, comparable in frequency to ubiquitinylation.
  • Understanding the substrate recognition mechanisms of the nine distinct human protein arginine methyltransferases (PRMTs) remains a significant challenge in molecular biology.

Purpose of the Study:

  • To review the progress made in understanding how human PRMTs recognize their protein targets.
  • To consolidate current knowledge on the biochemical mechanisms underlying PRMT substrate specificity.

Main Methods:

  • Structural biology techniques to visualize PRMT-substrate interactions.
  • Substrate profiling to identify in vivo and in vitro targets.
  • Bioorthogonal chemistry for activity-based protein profiling.
  • Proteomics approaches for large-scale target identification.

Main Results:

  • Recent advances have shed light on the molecular basis of PRMT substrate recognition.
  • Multiple lines of evidence from diverse methodologies are converging to explain target specificity.
  • The review synthesizes findings from structural, chemical, and biological approaches.

Conclusions:

  • Significant progress has been achieved in deciphering PRMT target recognition over the past decade.
  • A combination of advanced techniques is crucial for fully understanding these complex interactions.
  • Further research integrating these methods will continue to unravel the intricacies of protein arginine methylation.