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学術論文

Structure and Mechanism of RNA Polymerase II CTD Phosphatases

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Meinhart, Anton
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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引用

Kamenski, T., Heilmeier, S., Meinhart, A., & Cramer, P. (2004). Structure and Mechanism of RNA Polymerase II CTD Phosphatases. Molecular Cell, 15(3), 399-407. doi:10.1016/j.molcel.2004.06.035.

要旨

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