Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex

Nat Struct Mol Biol. 2018 Feb;25(2):135-138. doi: 10.1038/s41594-017-0020-6. Epub 2018 Jan 22.

Abstract

Mammalian mRNA biogenesis requires specific recognition of a hexanucleotide AAUAAA motif in the polyadenylation signals (PAS) of precursor mRNA (pre-mRNA) transcripts by the cleavage and polyadenylation specificity factor (CPSF) complex. Here we present a 3.1-Å-resolution cryo-EM structure of a core CPSF module bound to the PAS hexamer motif. The structure reveals the molecular interactions responsible for base-specific recognition, providing a rationale for mechanistic differences between mammalian and yeast 3' polyadenylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Cleavage And Polyadenylation Specificity Factor / chemistry*
  • Cryoelectron Microscopy
  • Humans
  • Image Processing, Computer-Assisted
  • Molecular Structure
  • Motion
  • Nuclear Proteins / chemistry
  • Poly A / chemistry
  • Polyadenylation*
  • Protein Binding
  • Protein Domains
  • Protein Multimerization
  • RNA Precursors / chemistry*
  • RNA, Messenger / chemistry

Substances

  • Cleavage And Polyadenylation Specificity Factor
  • Nuclear Proteins
  • RNA Precursors
  • RNA, Messenger
  • Poly A