Poly(A)-binding protein binds to A-rich sequences via RNA-binding domains 1+2 and 3+4

RNA Biol. 2006 Oct;3(4):170-7. doi: 10.4161/rna.3.4.4075. Epub 2006 Oct 26.

Abstract

Poly(A) binding protein (PABP) binds non-protein-coding BC1 RNA and BC200 RNA, which contain adenosine-rich domains. Two combinations of the four PABP RNA recognition motifs (RRMs), RRMs 1+2 and RRMs 3+4, bind with very strong affinities to various transcripts with long stretches of adenosine residues, whereas RRMs 2+3 bind weakly. While RRMs 1+2 preferentially bind to stretches that contain only adenosines, RRMs 3+4 exhibit relatively high affinities towards sequences that are interspersed with other nucleotides. Binding studies with oligoribonucleotide(A)(65) and oligoribonucleotide(A)(25) showed that the shorter RNA is not an ideal substrate for binding studies to model the interactions with mRNAs, which in general harbor long poly(A) tails.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine / metabolism*
  • Base Sequence
  • Binding Sites / genetics
  • Electrophoretic Mobility Shift Assay
  • Molecular Sequence Data
  • Poly(A)-Binding Proteins / metabolism*
  • Polymers / metabolism*
  • Protein Binding / genetics
  • Protein Structure, Tertiary / genetics
  • RNA, Small Cytoplasmic / metabolism*

Substances

  • BC1 RNA
  • Poly(A)-Binding Proteins
  • Polymers
  • RNA, Small Cytoplasmic
  • polyadenosine
  • Adenosine