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. 2022 Feb 1;36(3-4):195–209. doi: 10.1101/gad.349217.121

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© 2022 Schmidt et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 5. — Composition of CstF and mPSF, active in pre-mRNA cleavage. (A, left) Different versions of CstF and its subunits were analyzed by SDS-PAGE and Coomassie staining. “Canonical” subunits, including CstF64, are labeled with black arrows. CstF64τ is labeled with a gray arrow. (Right) CstF (64/τ) with a FLAG tag on CstF64τ and, as a control, CstF (64/64) without a FLAG tag were used in a FLAG pull-down experiment. (I) Input, (FT) flowthrough (E1 and E2) FLAG peptide eluates, (B) material remaining on the beads eluted with SDS sample buffer. Proteins were detected by Coomassie staining. The identity of the band running at the CstF64τ position in CstF (64/64) is unknown; based on Western blots, it is neither 64τ nor a fragment of CstF77. (B) Both CstF64 and 64τ are active in pre-mRNA cleavage, and CstF50 is essential. Proteins shown in A and their combinations were tested in cleavage assays. (C) Both mCF3 and mCF4 function in pre-mRNA cleavage. The two protein complexes, each with wild-type (+) or point-mutated (−) CPSF73, were combined with the remaining cleavage factors and tested in cleavage assays. The SV40 late Δ RNA served as negative control.