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Reconstitution of mammalian Cleavage Factor II involved in 3' processing of mRNA precursors

By Peter Schäfer, Christian Tüting, Lars Schönemann, Uwe Kühn, Thomas Treiber, Nora Treiber, Christian Ihling, Anne Graber, Walter Keller, Gunter Meister, Andrea Sinz, Elmar Wahle

Posted 10 Jul 2018
bioRxiv DOI: 10.1101/366336 (published DOI: 10.1261/rna.068056.118)

Cleavage factor II (CF II) is a poorly characterized component of the multi-protein complex catalyzing 3' cleavage and polyadenylation of mammalian mRNA precursors. We have reconstituted CF II as a heterodimer of hPcf11 and hClp1. The heterodimer is active in partially reconstituted cleavage reactions, whereas hClp1 by itself is not. Pcf11 moderately stimulates the RNA 5' kinase activity of hClp1; the kinase activity is dispensable for RNA cleavage. CF II binds RNA with nanomolar affinity. Binding is mediated mostly by the two zinc fingers in the C-terminal region of hPcf11. RNA is bound without pronounced sequence-specificity, but extended G-rich sequences appear to be preferred. We discuss the possibility that CF II contributes to the recognition of cleavage/polyadenylation substrates through interaction with G-rich far-downstream sequence elements.

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