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The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters

Academic Article
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Overview

authors

  • Ferdous, A.
  • Sikder, D.
  • Gillette, T.
  • Nalley, K.
  • Kodadek, Thomas
  • Johnston, S. A.

publication date

  • January 2007

journal

  • Genes & Development  Journal

abstract

  • Recent studies have shown that the intersection between transcription and proteins involved in the ubiquitin-proteasome pathway encompasses both proteolytic and nonproteolytic functions. Examples of the latter type include evidence that monoubiquitylation of some transcriptional activators stimulates their activity. In addition, the proteasomal ATPases are recruited to many active promoters through binding to activators and play an important, nonproteolytic role in promoter escape and elongation. In this study, we report the discovery of a new nonproteolytic activity of the proteasome (specifically the proteasomal ATPases): the active destabilization of activator-promoter complexes. This reaction depends on the presence of an activation domain and ATP. Destabilization is inhibited in vitro and in vivo if the protein is monoubiquitylated or if ubiquitin is genetically fused to the activator. The fact that monoubiquitylated activator is resistant to the "stripping" activity of the proteasomal ATPases may explain, in part, why some activators require this modification in order to function efficiently.

subject areas

  • Adenosine Triphosphatases
  • Adenosine Triphosphate
  • Blotting, Western
  • Chromatin Immunoprecipitation
  • DNA-Binding Proteins
  • Gene Expression Regulation, Fungal
  • HeLa Cells
  • Humans
  • Promoter Regions, Genetic
  • Proteasome Endopeptidase Complex
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • TATA Box
  • Trans-Activators
  • Transcription Factors
  • Transcription, Genetic
  • Transcriptional Activation
  • Ubiquitin
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Research

keywords

  • Gal4
  • Sug1
  • promoter occupancy
  • proteasome
  • transcription
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Identity

PubMed Central ID

  • PMC1759896

International Standard Serial Number (ISSN)

  • 0890-9369

Digital Object Identifier (DOI)

  • 10.1101/gad.1493207

PubMed ID

  • 17167105
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Additional Document Info

start page

  • 112

end page

  • 123

volume

  • 21

issue

  • 1

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