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Recruitment of a 19s proteasome subcomplex to an activated promoter

Academic Article
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Overview

authors

  • Gonzalez, F.
  • Delahodde, A.
  • Kodadek, Thomas
  • Johnston, S. A.

publication date

  • April 2002

journal

  • Science  Journal

abstract

  • The 19S proteasome regulatory particle plays a critical role in cellular proteolysis. However, recent reports have demonstrated that 19S proteins play a nonproteolytic role in nucleotide excision repair and transcription elongation. We show by chromatin immunoprecipitation assays that proteins comprising the 19S complex are recruited to the GAL1-10 promoter by the Gal4 transactivator upon induction with galactose. This recruited complex does not contain proteins from the 20S proteolytic particle and includes a subset of the 19S proteins. This subset is also specifically retained from an extract by the Gal4 activation domain. These data indicate that in vivo, the base of the 19S complex functions independently of the larger complex and plays a direct, nonproteolytic role in RNA polymerase II transcription.

subject areas

  • Adenosine Triphosphatases
  • Cysteine Endopeptidases
  • DNA, Fungal
  • DNA-Binding Proteins
  • Endopeptidases
  • Fungal Proteins
  • Galactose
  • Gene Expression Regulation, Fungal
  • Multienzyme Complexes
  • Mutation
  • Precipitin Tests
  • Promoter Regions, Genetic
  • Proteasome Endopeptidase Complex
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Transcription, Genetic
  • Ubiquitin
  • Yeasts
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1069490

PubMed ID

  • 11964484
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Additional Document Info

start page

  • 548

end page

  • 550

volume

  • 296

issue

  • 5567

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