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Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1

Academic Article
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Overview

authors

  • Zhang, Yan Jessie
  • Ki, Y.
  • Genoud, N.
  • Gao, J. M.
  • Kelly, Jeffery
  • Pfaff, S. L.
  • Gill, G. N.
  • Dixon, J. E.
  • Noel, J. P.

publication date

  • December 2006

journal

  • Molecular Cell  Journal

abstract

  • Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. Fcp1 and Scp1 belong to a family of Mg2+ -dependent phosphoserine (P.Ser)/phosphothreonine (P.Thr)-specific phosphatases. We recently showed that Scp1 is an evolutionarily conserved regulator of neuronal gene silencing. Here, we present the X-ray crystal structures of a dominant-negative form of human Scp1 (D96N mutant) bound to mono- and diphosphorylated peptides encompassing the CTD heptad repeat (Y1S2P3T4S5P6S7). Moreover, kinetic and thermodynamic analyses of Scp1-phospho-CTD peptide complexes support the structures determined. This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. Moreover, these results provide a template for the design of specific inhibitors of Scp1 for the study of neuronal stem cell development.

subject areas

  • Crystallography, X-Ray
  • Humans
  • Kinetics
  • Models, Molecular
  • Nuclear Proteins
  • Peptides
  • Phosphoprotein Phosphatases
  • Phosphorylation
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • RNA Polymerase II
  • Terminal Repeat Sequences
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Identity

PubMed Central ID

  • PMC2859291

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2006.10.027

PubMed ID

  • 17157258
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Additional Document Info

start page

  • 759

end page

  • 770

volume

  • 24

issue

  • 5

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