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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2001-6-11
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pubmed:abstractText |
In addition to a role in DNA repair events in yeast, several lines of evidence indicate that the Rad23 protein (Rad23p) may regulate the activity of the 26 S proteasome. We report evidence that a de-N-glycosylating enzyme, Png1p, may be involved in the proteasomal degradation pathway via its binding to Rad23p. Interaction of Rad23p and Png1p was first detected by two-hybrid screening, and this interaction in vivo was confirmed by biochemical analyses. The Png1p-Rad23p complex was shown to be distinct from the well established DNA repair complex, Rad4p-Rad23p. We propose a model in which Rad23p functions as an escort protein to link the 26 S proteasome with proteins such as Rad4p or Png1p to regulate their cellular activities.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP dependent 26S protease,
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide-N4-(N-acetyl-beta-glucosamin...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/RAD23 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21601-7
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pubmed:dateRevised |
2009-7-24
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pubmed:meshHeading |
pubmed-meshheading:11259433-Amidohydrolases,
pubmed-meshheading:11259433-Base Sequence,
pubmed-meshheading:11259433-Chromatography, Gel,
pubmed-meshheading:11259433-Cloning, Molecular,
pubmed-meshheading:11259433-Cytosol,
pubmed-meshheading:11259433-DNA, Fungal,
pubmed-meshheading:11259433-DNA Primers,
pubmed-meshheading:11259433-DNA Repair,
pubmed-meshheading:11259433-DNA-Binding Proteins,
pubmed-meshheading:11259433-Escherichia coli,
pubmed-meshheading:11259433-Fungal Proteins,
pubmed-meshheading:11259433-Glycosylation,
pubmed-meshheading:11259433-Models, Biological,
pubmed-meshheading:11259433-Molecular Sequence Data,
pubmed-meshheading:11259433-Peptide Hydrolases,
pubmed-meshheading:11259433-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase,
pubmed-meshheading:11259433-Plasmids,
pubmed-meshheading:11259433-Proteasome Endopeptidase Complex,
pubmed-meshheading:11259433-Recombinant Proteins,
pubmed-meshheading:11259433-Saccharomyces cerevisiae,
pubmed-meshheading:11259433-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11259433-Ultraviolet Rays
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pubmed:year |
2001
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pubmed:articleTitle |
Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast.
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pubmed:affiliation |
Department of Biochemistry, Institute for Cell and Developmental Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-5215, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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