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Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome

Academic Article
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Overview

authors

  • Verma, R.
  • Aravind, L.
  • Oania, R.
  • McDonald, W. H.
  • Yates III, John
  • Koonin, E. V.
  • Deshaies, R. J.

publication date

  • October 2002

journal

  • Science  Journal

abstract

  • The 26S proteasome mediates degradation of ubiquitin-conjugated proteins. Although ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at the proteasome and its relation to substrate degradation remain unknown. The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated metalloisopeptidase (JAMM) motif-EX(n)HXHX(10)D. Mutation of the predicted active-site histidines to alanine (rpn11AXA) was lethal and stabilized ubiquitin pathway substrates in yeast. Rpn11(AXA) mutant proteasomes assembled normally but failed to either deubiquitinate or degrade ubiquitinated Sic1 in vitro. Our findings reveal an unexpected coupling between substrate deubiquitination and degradation and suggest a unifying rationale for the presence of the lid in eukaryotic proteasomes.

subject areas

  • Adenosine Triphosphate
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Carbon-Nitrogen Lyases
  • Cyclin-Dependent Kinase Inhibitor Proteins
  • Cysteine Endopeptidases
  • DNA-Binding Proteins
  • Endopeptidases
  • Fungal Proteins
  • Metalloendopeptidases
  • Molecular Sequence Data
  • Multienzyme Complexes
  • Mutation
  • Oligopeptides
  • Peptide Hydrolases
  • Proteasome Endopeptidase Complex
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Ubiquitins
  • Yeasts
  • Zinc
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1075898

PubMed ID

  • 12183636
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Additional Document Info

start page

  • 611

end page

  • 615

volume

  • 298

issue

  • 5593

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