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Structural basis for RNA recognition by a type II poly(A)-binding protein.

Jikui Song1, Jered V McGivern, Karl W Nichols

  • 1Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin, Madison, WI 53706, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 1, 2008
PubMed
Summary

Xenopus laevis embryonic type II poly(A)-binding protein (XlePABP2) forms a homodimer. Upon binding poly(A), it transitions to a monomer, revealing the RNA recognition site for gene regulation.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Type II poly(A)-binding proteins (PABPs) play crucial roles in mRNA processing and regulation.
  • Understanding the structural basis of PABP function is essential for elucidating gene expression mechanisms.

Purpose of the Study:

  • To determine the high-resolution structure of the Xenopus laevis embryonic type II poly(A)-binding protein (XlePABP2) functional domain.
  • To investigate the mechanism of poly(A) recognition and RRM domain regulation in type II PABPs.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the structure of the XlePABP2-TRP domain.
  • Structural analysis focused on the homodimeric state and the transition upon poly(A) binding.

Main Results:

  • The XlePABP2-TRP domain forms a homodimer through antiparallel beta-strand association of its single RNA recognition motif (RRM) domain.
  • A polyproline motif occludes the canonical RNA binding site in the homodimeric state.
  • Poly(A) binding induces a dimer-to-monomer transition, freeing the RRM site for adenosine nucleotide binding.

Conclusions:

  • This study provides high-resolution structural insights into type II PABPs.
  • XlePABP2 represents a novel example of a single RRM domain protein switching from a homodimer to a monomer upon RNA binding.
  • These findings enhance understanding of RRM domain regulation, poly(A) recognition, and type II PABP function in mRNA processing and disease.