Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast

Audrey Perreault1, Caroline Lemieux, François Bachand

  • 1Department of Biochemistry, Université de Sherbrooke, Québec J1H 5N4, Canada.

Insights

Fission yeast Pab2 protein binds poly(A) tails and is essential for mRNA regulation. Arginine methylation by RMT1 controls Pab2

Area of Science:

  • Molecular Biology
  • RNA Metabolism
  • Post-translational Modifications

Background:

  • Mammalian cells utilize distinct cytoplasmic and nuclear poly(A)-binding proteins (PABP).
  • A functional homolog of the nuclear PABP2 in yeast remained unidentified.
  • Arginine methylation is a key post-translational modification with regulatory roles.

Purpose of the Study:

  • To identify and characterize a yeast homolog of mammalian PABP2.
  • To investigate the role of this protein in mRNA poly(A) tail metabolism.
  • To explore the impact of arginine methylation on Pab2 function.

Main Methods:

  • Identification of a PABP2 homolog in fission yeast (Schizosaccharomyces pombe) named Pab2.
  • In vitro poly(A) binding assays to confirm Pab2's RNA-binding capability.
  • Analysis of mRNA 3'-end lengths in pab2-null cells.
  • Investigation of RMT1-dependent arginine methylation of Pab2.
  • Assessment of Pab2 oligomerization and growth phenotypes in wild-type and mutant cells.

Main Results:

  • Fission yeast Pab2 is a nonessential nuclear protein that specifically binds poly(A) RNA.
  • pab2-null cells exhibit hyperadenylated mRNA 3'-ends, indicating a role in poly(A) tail length control.
  • Pab2's C-terminal arginine residues are methylated by RMT1, influencing Pab2 oligomerization.
  • Non-methylated Pab2 shows increased oligomerization, and Pab2 overexpression inhibits growth, exacerbated in rmt1-null cells.

Conclusions:

  • Fission yeast Pab2 functions in poly(A) tail length control.
  • Arginine methylation by RMT1 regulates Pab2 oligomerization.
  • This study reveals a biological role for arginine methylation in modulating Pab2 activity.

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