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Physical and functional association of RNA polymerase II and the proteasome

Academic Article
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Overview

authors

  • Gillette, T. G.
  • Gonzalez, F.
  • Delahodde, A.
  • Johnston, S. A.
  • Kodadek, Thomas

publication date

  • April 2004

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Recent studies from a number of laboratories have revealed a surprising number of connections between RNA polymerase II transcription and the ubiquitin/proteasome pathway. We now find yet another intersection of these pathways by showing that the 26S proteasome associates with regions of the GAL1, GAL10, and HSP82 genes, including the 3' ends, in a transcription-dependent fashion. The appearance of the proteasome on these inducible genes correlates with both the accumulation of transcripts and the buildup of RNA polymerase II complexes in the same region. Furthermore, the 26S proteasome and RNA polymerase II coimmunoprecipitate, and inhibition of 26S proteolytic activity leads to increased read through of a transcription termination site. We suggest that the proteasome is generally recruited to the DNA at sites of stalled RNA polymerase and may act to resolve these complexes.

subject areas

  • Cysteine Endopeptidases
  • Hydrolysis
  • Multienzyme Complexes
  • Precipitin Tests
  • Proteasome Endopeptidase Complex
  • RNA Polymerase II
  • Transcription, Genetic
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Identity

PubMed Central ID

  • PMC395896

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0305411101

PubMed ID

  • 15069196
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Additional Document Info

start page

  • 5904

end page

  • 5909

volume

  • 101

issue

  • 16

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