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The gal4 activation domain binds sug2 protein, a proteasome component, in vivo and in vitro

Academic Article
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Overview

authors

  • Chang, C.
  • Gonzalez, F.
  • Rothermel, B.
  • Sun, L. P.
  • Johnston, S. A.
  • Kodadek, Thomas

publication date

  • August 2001

journal

  • Journal of Biological Chemistry  Journal

abstract

  • An in vivo protein interaction assay was used to search a yeast cDNA library for proteins that bind to the acidic activation domain (AD) of the yeast Gal4 protein. Sug2 protein, a component of the 19 S regulatory particle of the 26 S proteasome, was one of seven proteins identified in this screen. In vitro binding assays confirm a direct interaction between these proteins. SUG2 and SUG1, another 19 S component, were originally discovered as a mutation able to suppress the phenotype of a Gal4 truncation mutant (Gal4(D)p) lacking much of its AD. Sug1p has previously been shown to bind the Gal4 AD in vitro. Taken together, these genetic and biochemical data suggest a biologically significant interaction between the Gal4 protein and the 19 S regulatory particle of the proteasome. Indeed, it is demonstrated here that the Gal4 AD interacts specifically with immunopurified 19 S complex. The proteasome regulatory particle has been shown recently to play a direct role in RNA polymerase II transcription and the activator-19 S interaction could be important in recruiting this large complex to transcriptionally active GAL genes.

subject areas

  • Adenosine Triphosphatases
  • Animals
  • Benzamides
  • Binding Sites
  • Cysteine Endopeptidases
  • DNA-Binding Proteins
  • Dimerization
  • Fungal Proteins
  • Multienzyme Complexes
  • Promoter Regions, Genetic
  • Proteasome Endopeptidase Complex
  • Rabbits
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Tyrosine
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M102254200

PubMed ID

  • 11418596
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Additional Document Info

start page

  • 30956

end page

  • 30963

volume

  • 276

issue

  • 33

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