The C terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3′-end processing
- Fan Yang1,
- Peter Hsu1,
- Susan D. Lee2,
- Wen Yang1,
- Derick Hoskinson2,
- Weihao Xu1,
- Claire Moore2 and
- Gabriele Varani1
- 1Department of Chemistry, University of Washington, Seattle, Washington 98195, USA
- 2Department of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA
- Corresponding author: varani{at}chem.washington.edu
Abstract
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.
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Article is online at http://www.rnajournal.org/cgi/doi/10.1261/rna.058354.116.
- Received July 20, 2016.
- Accepted October 16, 2016.
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