Grabbing the message: structural basis of mRNA 3'UTR recognition by Hrp1

EMBO J. 2006 Jul 12;25(13):3167-78. doi: 10.1038/sj.emboj.7601190. Epub 2006 Jun 22.


The recognition of specific signals encoded within the 3'-untranslated region of the newly transcribed mRNA triggers the assembly of a multiprotein machine that modifies its 3'-end. Hrp1 recognises one of such signals, the so-called polyadenylation enhancement element (PEE), promoting the recruitment of other polyadenylation factors in yeast. The molecular bases of this interaction are revealed here by the solution structure of a complex between Hrp1 and an oligonucleotide mimicking the PEE. Six consecutive bases (AUAUAU) are specifically recognised by two RNA-binding domains arranged in tandem. Both protein and RNA undergo significant conformational changes upon complex formation with a concomitant large surface burial of RNA bases. Key aspects of RNA specificity can be explained by the presence of intermolecular aromatic-aromatic contacts and hydrogen bonds. Altogether, the Hrp1-PEE structure represents one of the first steps towards understanding of the assembly of the cleavage and polyadenylation machinery at the atomic level.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3' Untranslated Regions*
  • Adenine / chemistry
  • Amino Acid Sequence
  • Hydrogen Bonding
  • Models, Molecular*
  • Molecular Sequence Data
  • Mutation
  • Nucleic Acid Conformation
  • Polyadenylation
  • Protein Binding
  • RNA, Messenger / chemistry*
  • Ribose / chemistry
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Uracil / chemistry
  • mRNA Cleavage and Polyadenylation Factors / chemistry*
  • mRNA Cleavage and Polyadenylation Factors / genetics


  • 3' Untranslated Regions
  • HRP1 protein, S cerevisiae
  • RNA, Messenger
  • Saccharomyces cerevisiae Proteins
  • mRNA Cleavage and Polyadenylation Factors
  • Uracil
  • Ribose
  • Adenine