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RNA. 2017 Jan;23(1):98-107. Epub 2016 Oct 25.

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

Author information

1
Department of Chemistry, University of Washington, Seattle, Washington 98195, USA.
2
Department of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.

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.

KEYWORDS:

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

PMID:
27780845
PMCID:
PMC5159653
DOI:
10.1261/rna.058354.116
[Indexed for MEDLINE]
Free PMC Article

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