2nax | pdb_00002nax
Structure of CCHC zinc finger domain of Pcf11
Structural highlights
Function[PCF11_YEAST] Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.[1] [2] Publication Abstract from PubMed3'-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, multi-domain 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 co-transcriptional RNA processing. The C-terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'- end processing.,Yang F, Hsu P, Lee SD, Yang W, Hoskinson D, Xu W, Moore C, Varani G RNA. 2016 Oct 25. pii: rna.058354.116. PMID:27780845[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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