Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5593
pubmed:dateCreated
2002-10-18
pubmed:abstractText
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.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ATP dependent 26S protease, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Nitrogen Lyases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor..., http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/RPN11 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SIC1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins, http://linkedlifedata.com/resource/pubmed/chemical/Zinc, http://linkedlifedata.com/resource/pubmed/chemical/epoxomicin, http://linkedlifedata.com/resource/pubmed/chemical/isopeptidase
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
298
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
611-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12183636-Adenosine Triphosphate, pubmed-meshheading:12183636-Amino Acid Motifs, pubmed-meshheading:12183636-Amino Acid Sequence, pubmed-meshheading:12183636-Binding Sites, pubmed-meshheading:12183636-Carbon-Nitrogen Lyases, pubmed-meshheading:12183636-Cyclin-Dependent Kinase Inhibitor Proteins, pubmed-meshheading:12183636-Cysteine Endopeptidases, pubmed-meshheading:12183636-DNA-Binding Proteins, pubmed-meshheading:12183636-Endopeptidases, pubmed-meshheading:12183636-Fungal Proteins, pubmed-meshheading:12183636-Metalloendopeptidases, pubmed-meshheading:12183636-Molecular Sequence Data, pubmed-meshheading:12183636-Multienzyme Complexes, pubmed-meshheading:12183636-Mutation, pubmed-meshheading:12183636-Oligopeptides, pubmed-meshheading:12183636-Peptide Hydrolases, pubmed-meshheading:12183636-Proteasome Endopeptidase Complex, pubmed-meshheading:12183636-Saccharomyces cerevisiae Proteins, pubmed-meshheading:12183636-Transcription Factors, pubmed-meshheading:12183636-Ubiquitins, pubmed-meshheading:12183636-Yeasts, pubmed-meshheading:12183636-Zinc
pubmed:year
2002
pubmed:articleTitle
Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome.
pubmed:affiliation
Department of Biology and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't