The 30-kd subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are rna-binding zinc finger proteins

Silvia M.L. Barabino, Wolfgang Hübner, Andreas Jenny, Lionel Minvielle-Sebastia, Walter Keller

Research output: Contribution to journalArticlepeer-review

150 Scopus citations

Abstract

Cleavage and polyadenylation specificity factor (CPSF), a key component of the mammalian RNA 3-end processing machinery, consists of four subunits of 160, 100, 73, and 30 kD. Here we report the isolation and characterization of a cDNA encoding the 30-kD polypeptide. Antibodies raised against this protein inhibit cleavage and polyadenylation and coimmunoprecipitate the other CPSF subunits. The protein sequence contains five C3H-zinc-finger repeats and a putative RNA-binding zinc knuckle motif at the carboxyl terminus. Consistent with this observation, the in vitro translated 30-kD protein binds RNA polymers with a distinct preference for poly(U). In addition, an essential S. cerevisiae gene, YTH1, was cloned which is 40% identical to CPSF 30K at the protein level. Extracts prepared from a conditional yth1 mutant have normal cleavage activity, but fail to polyadenylate the upstream cleavage product. Efficient polyadenylation activity can be restored by the addition of purified polyadenylation factor I (PF I). We demonstrate that Yth1p is a component of PF I that interacts in vivo and in vitro with Fip1p, a known PF I subunit.

Original languageEnglish (US)
Pages (from-to)1703-1716
Number of pages14
JournalGenes and Development
Volume11
Issue number13
DOIs
StatePublished - Jul 1 1997
Externally publishedYes

Keywords

  • Cleavage and polyadenylation specificity factor
  • Polyadenylation factor I
  • Pre-mRNA processing
  • Yeast
  • Zinc finger
  • Zinc knuckle

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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