The C terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'-end processing

RNA. 2017 Jan;23(1):98-107. doi: 10.1261/rna.058354.116. Epub 2016 Oct 25.


3'-End processing of pre-mRNAs prior to packaging and export to the cytoplasm of the mature transcript is a highly regulated process executed by several tens of protein factors that recognize poorly conserved RNA signals. Among them is Pcf11, a highly conserved, multidomain protein that links transcriptional elongation, 3'-end processing, and transcription termination. Here we report the structure and biochemical function of Pcf11's C-terminal domain, which is conserved from yeast to humans. We identify a novel zinc-finger fold, resembling a trillium flower. Structural, biochemical, and genetic analyses reveal a highly conserved surface that plays a critical role in both cleavage and polyadenylation. These findings provide further insight into this important protein and its multiple functional roles during cotranscriptional RNA processing.

Keywords: NMR; Pcf11; mRNA 3′-end processing; structure; zinc finger.

MeSH terms

  • Amino Acid Sequence
  • Conserved Sequence
  • Gene Expression Regulation, Fungal
  • Models, Molecular
  • Polyadenylation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA Cleavage
  • RNA, Messenger / genetics*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription, Genetic
  • Zinc Fingers
  • mRNA Cleavage and Polyadenylation Factors / chemistry*
  • mRNA Cleavage and Polyadenylation Factors / genetics
  • mRNA Cleavage and Polyadenylation Factors / metabolism*


  • PCF11 protein, S cerevisiae
  • RNA, Messenger
  • Saccharomyces cerevisiae Proteins
  • mRNA Cleavage and Polyadenylation Factors