Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast.
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.
Mesh Terms:
Amidohydrolases, Base Sequence, Chromatography, Gel, Cloning, Molecular, Cytosol, DNA Primers, DNA Repair, DNA, Fungal, DNA-Binding Proteins, Escherichia coli, Fungal Proteins, Glycosylation, Models, Biological, Molecular Sequence Data, Peptide Hydrolases, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Plasmids, Proteasome Endopeptidase Complex, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ultraviolet Rays
Amidohydrolases, Base Sequence, Chromatography, Gel, Cloning, Molecular, Cytosol, DNA Primers, DNA Repair, DNA, Fungal, DNA-Binding Proteins, Escherichia coli, Fungal Proteins, Glycosylation, Models, Biological, Molecular Sequence Data, Peptide Hydrolases, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Plasmids, Proteasome Endopeptidase Complex, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Ultraviolet Rays
J. Biol. Chem.
Date: Jun. 15, 2001
PubMed ID: 11259433
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