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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

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Arginine methylation and citrullination of splicing factor proline- and glutamine-rich (SFPQ/PSF) regulates its

Ambrosius P Snijders1, Guillaume M Hautbergue2, Alex Bloom3

  • 1ChELSI Institute, Chemical and Biological Engineering, University of Sheffield, Sheffield S1 3JD, United Kingdom.

RNA (New York, N.Y.)
|January 22, 2015
PubMed

Insights

Splicing factor SFPQ/PSF and NONO form a complex influencing RNA processing. Arginine methylation of SFPQ/PSF enhances mRNA binding, impacting mRNP dynamics.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Splicing factor proline- and glutamine-rich (SFPQ/PSF) and non-POU domain-containing octamer-binding protein (NONO) form a nuclear protein complex.
  • The precise functions of the SFPQ/NONO complex in cellular processes remain incompletely understood.
  • This complex is known to be involved in RNA processing, splicing, and transcriptional regulation.

Purpose of the Study:

  • To elucidate the multifunctional roles of the SFPQ/NONO complex.
  • To identify post-translational modifications of SFPQ/PSF and their impact on complex function.
  • To investigate the influence of purification conditions on the SFPQ/NONO complex's biochemical properties.

Main Methods:

  • Purification of the endogenous SFPQ/NONO complex.
  • Mass spectrometry to identify interacting proteins and post-translational modifications (arginine methylation, citrullination).
  • In vitro enzymatic assays using PRMT1 and in vivo studies in mammalian cells.

Main Results:

  • Mass spectrometry identified numerous proteins involved in RNA processing and splicing interacting with SFPQ/NONO.
  • Several sites of asymmetric arginine dimethylation were identified in SFPQ/PSF, catalyzed by PRMT1 and antagonized by citrullination.
  • Arginine methylation of SFPQ/PSF increased its association with mRNA in mRNP complexes without affecting NONO binding.
  • Low ionic strength during purification led to the formation of large, heterogeneous SFPQ/NONO protein assemblies, hindering purification.

Conclusions:

  • The SFPQ/NONO complex plays a significant role in RNA processing, splicing, and transcriptional regulation.
  • Post-translational modifications, specifically arginine methylation of SFPQ/PSF, modulate its interaction with mRNA and influence mRNP dynamics.
  • The ability of the SFPQ/NONO complex to form dynamic protein assemblies is sensitive to biochemical conditions, impacting its study and function.
Keywords:
arginine methylationcitrullinationmRNP bindingmass spectrometrynon-POU domain-containing octamer-binding proteinpolypyrimidine tract-binding protein-associated-splicing factorsplicing factor proline- and glutamine-rich

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