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Cks1-dependent proteasome recruitment and activation of cdc20 transcription in budding yeast

Academic Article
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Overview

authors

  • Morris, M. C.
  • Kaiser, P.
  • Rudyak, S.
  • Baskerville, C.
  • Watson, M. H.
  • Reed, Steven

publication date

  • June 2003

journal

  • Nature  Journal

abstract

  • Cks proteins are small evolutionarily conserved proteins that interact genetically and physically with cyclin-dependent kinases. However, in spite of a large body of genetic, biochemical and structural research, no compelling unifying model of their functions has emerged. Here we show, by investigating the essential role of Cks1 in Saccharomyces cerevisiae, that the protein is primarily involved in promoting mitosis by modulating the transcriptional activation of the APC/C protein-ubiquitin ligase activator Cdc20. Cks1 is required for both the periodic dissociation of Cdc28 kinase from the CDC20 promoter and the periodic association of the proteasome with the promoter. We propose that the essential role of Cks1 is to recruit the proteasome to, and/or dissociate the Cdc28 kinase from, the CDC20 promoter, thus facilitating transcription by remodelling transcriptional complexes or chromatin associated with the CDC20 gene.

subject areas

  • Adaptor Proteins, Signal Transducing
  • CDC28 Protein Kinase, S cerevisiae
  • Cdc20 Proteins
  • Cell Cycle Proteins
  • Cysteine Endopeptidases
  • Gene Expression Regulation, Fungal
  • Multienzyme Complexes
  • Promoter Regions, Genetic
  • Proteasome Endopeptidase Complex
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/nature01720

PubMed ID

  • 12827207
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Additional Document Info

start page

  • 1009

end page

  • 1013

volume

  • 423

issue

  • 6943

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