Structure and mechanism of RNA polymerase IICTD phosphatases.

Kamenski, T.; Heilmeier, S.; Meinhart, A.; Cramer, P.

doi:10.1016/j.molcel.2004.06.035

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Structure and mechanism of RNA polymerase IICTD phosphatases.

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Cramer, P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Kamenski, T., Heilmeier, S., Meinhart, A., & Cramer, P. (2004). Structure and mechanism of RNA polymerase IICTD phosphatases. Molecular Cell, 15(3), 399-407. doi:10.1016/j.molcel.2004.06.035.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-84E6-3

Abstract

Recycling of RNA polymerase II (Pol II) after transcription requires dephosphorylation of the polymerase C-terminal domain (CTD) by the phosphatase Fcp1. We report the X-ray structure of the small CTD phosphatase Scp1, which is homologous to the Fcp1 catalytic domain. The structure shows a core fold and an active center similar to those of phosphotransferases and phosphohydrolases that solely share a DXDX(V/T) signature motif with Fcp1/Scp1. We demonstrate that the first aspartate in the signature motif undergoes metal-assisted phosphorylation during catalysis, resulting in a phosphoaspartate intermediate that was structurally mimicked with the inhibitor beryllofluoride. Specificity may result from CTD binding to a conserved hydrophobic pocket between the active site and an insertion domain that is unique to Fcp1/Scp1. Fcp1 specificity may additionally arise from phosphatase recruitment near the CTD via the Pol II subcomplex Rpb4/7, which is shown to be required for binding of Fcp1 to the polymerase in vitro.