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. 2018 Sep 26;46(22):12022–12039. doi: 10.1093/nar/gky862

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — CstF-64 stimulates cleavage and polyadenylation in correlation to the amount of CstF-64 protein produced in SLAP. (A) Schematic representation of the coat binding protein from bacteriophage MS2 (MCP) fused to human CstF-64 (MCP-CstF-64). Functional domains in CstF-64 and three FLAG tags are indicated. (B) Schematic representation of the reporter construct (SL-Luc) containing the Renilla luciferase and two MS2 stem-loop (SL) sequences downstream of the cleavage and polyadenylation site. (C) The interaction between MCP-CstF-64 and the SL-Luc reporter construct is mediated through the interaction between MCP and MS2 stem-loops. (D) SLAP results showing NLUs in HeLa cells without MCP-CstF-64 (–), and in cells transfected with increasing amounts of MCP-CstF-64. Western blots with the designated antibodies to show the expression of the FLAG-tagged version of MCP-CstF-64 (WB: FLAG) and endogenous CstF-64 (WB: CSTF2). β-tubulin was used as a loading control. A bar graph of the quantified expression of MCP-CstF-64 normalized to β-tubulin (bottom). (E) A linear regression between the amount of MCP-CstF-64 protein normalized to β-tubulin (x-axis) to the NLU from SLAP (y-axis). The correlation value (R² = 0.99548) is shown.