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

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.
Mesh Terms:
Amino Acid Sequence, Conserved Sequence, Gene Expression Regulation, Fungal, Models, Molecular, Polyadenylation, Protein Structure, Secondary, Protein Structure, Tertiary, RNA Cleavage, RNA, Messenger, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription, Genetic, Zinc Fingers, mRNA Cleavage and Polyadenylation Factors
RNA
Date: Jan. 01, 2017
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