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  Structure and mechanism of RNA polymerase IICTD phosphatases.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-84E6-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-D721-0
Genre: Journal Article

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1940659.pdf (Publisher version), 547KB
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Kamenski, T., Author
Heilmeier, S., Author
Meinhart, A., Author
Cramer, P.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 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.

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Language(s): eng - English
 Dates: 2004-08-13
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2004.06.035
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 15 (3) Sequence Number: - Start / End Page: 399 - 407 Identifier: -