Skip to main content
. Author manuscript; available in PMC: 2015 Jul 1.
Published in final edited form as: Mol Biosyst. 2014 Jul;10(7):1730–1741. doi: 10.1039/c4mb00109e

Fig. 3.

Fig. 3

Serine 217 phosphorylation does not alter the activity of Rtr1. (A) Mutation of serine 217 to aspartic acid does not alter the phosphatase activity of Rtr1. DiFMUP dephosphorylation assays were performed over a two-hour time course to measure the activity of WT (n = 6) and S217D (n = 9) Rtr1 relative to a GST alone control reaction. The amount of DiFMU produced over time is shown as an average ± standard deviation. (B) Serine 217 is not required for the interaction between RNAPII and Rtr1. TAP-tagged Rtr1 (WT, S217A, or S217D) was immunoprecipitated (IP) using IgG Sepharose resin. Input whole cell extract is shown in the panels to the left. Western blot analysis was performed to assess the interaction of Rtr1 (anti-TAP) with RNAPII. Rpb3 is a core subunit of RNAPII whereas the anti-SerP antibodies are all directed against specific modified forms of the Rpb1 C-terminal domain.