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Updated: Jul 14, 2026

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
09:04

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding

Nadeem Siddiqui1, David A Mangus, Tsung-Cheng Chang

  • 1Department of Biochemistry, McGill University, Montréal, Quebec H3G 1Y6, Canada.

The Journal of Biological Chemistry
|June 28, 2007
PubMed

Insights

Poly(A)-binding protein (PABP) recruits deadenylase enzymes to messenger complexes. This reveals a new role for PABP in mRNA processing, influencing maturation, export, and turnover.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Eukaryotic Gene Regulation

Background:

  • Poly(A)-binding protein (PABP) is crucial for eukaryotic translation, mRNA metabolism, and export.
  • PABP's PABC domain recruits proteins with PAM-2 motifs to messenger ribonucleoprotein complexes.
  • Several human proteins, including Paip1, Paip2, eRF3, Ataxin-2, and Tob2, interact with PABP to regulate translation.

Purpose of the Study:

  • To identify novel PABP-interacting partners.
  • To investigate the role of the PABC domain in recruiting specific protein complexes.
  • To elucidate the function of PABP in mRNA metabolic processes.

Main Methods:

  • Yeast and human cell-based interaction studies.
  • Identification of PAM-2 motifs within interacting proteins.
  • Analysis of protein-protein interactions using biochemical assays.

Main Results:

  • Poly(A) nuclease (PAN) was identified as a PABP-interacting partner in yeast and humans.
  • The interaction between PABP and PAN is mediated by a conserved PAM-2 motif in the PAN3 subunit.
  • PABP directly recruits a deadenylase complex to the messenger ribonucleoprotein complex.

Conclusions:

  • The PABC domain of PABP plays a novel role in recruiting deadenylases, linking PABP to mRNA turnover.
  • This interaction is conserved across fungal and animal species.
  • PABP is involved in mRNA maturation, export, and turnover, extending its known functions.

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