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Structure and Mechanism of RNA Polymerase II CTD Phosphatases
- Source :
-
Molecular Cell . Aug2004, Vol. 15 Issue 3, p399-407. 9p. - Publication Year :
- 2004
-
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. [Copyright &y& Elsevier]
- Subjects :
- *RNA polymerases
*SURFACE chemistry
*CHEMICAL reactions
*NUCLEIC acids
Subjects
Details
- Language :
- English
- ISSN :
- 10972765
- Volume :
- 15
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Molecular Cell
- Publication Type :
- Academic Journal
- Accession number :
- 14101543
- Full Text :
- https://doi.org/10.1016/j.molcel.2004.06.035