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Updated: Jul 17, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
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.
Abstract:
Two structurally different poly(A)-binding proteins (PABP) bind the poly(A) tract of mRNAs in most mammalian cells: PABPC in the cytoplasm and PABP2/PABPN1 in the nucleus. Whereas yeast orthologs of the cytoplasmic PABP are characterized, a gene product homologous to mammalian PABP2 has not been identified in yeast. We report here the identification of a homolog of PABP2 as an arginine methyltransferase 1 (RMT1)-associated protein in fission yeast. The product of the Schizosaccharomyces pombe pab2 gene encodes a nonessential nuclear protein and demonstrates specific poly(A) binding in vitro. Consistent with a functional role in poly(A) tail metabolism, mRNAs from pab2-null cells displayed hyperadenylated 3'-ends. We also show that arginine residues within the C-terminal arginine-rich domain of Pab2 are modified by RMT1-dependent methylation. Whereas the arginine methylated and unmethylated forms of Pab2 behaved similarly in terms of subcellular localization, poly(A) binding, and poly(A) tail length control; Pab2 oligomerization levels were markedly increased when Pab2 was not methylated. Significantly, Pab2 overexpression reduced growth rate, and this growth inhibitory effect was exacerbated in rmt1-null cells. Our results indicate that the main cellular function of Pab2 is in poly(A) tail length control and support a biological role for arginine methylation in the regulation of Pab2 oligomerization.
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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