Protein degradation: recognition of ubiquitinylated substrates.
A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a role.
Hartmann-Petersen
Rasmus
R
August Krogh Institute, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen, Denmark.
Gordon
Colin
C
D002352:Carrier Proteins / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000378:metabolism; D050756:Cyclin-Dependent Kinase Inhibitor Proteins; D004268:DNA-Binding Proteins / Q000378:metabolism; D008954:Models, Biological; D046988:Proteasome Endopeptidase Complex / Q000502:physiology*; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000378:metabolism; D014452:Ubiquitins / Q000378:metabolism* / Q000502:physiology*; D015003:Yeasts
D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D050756:Cyclin-Dependent Kinase Inhibitor Proteins; D004268:DNA-Binding Proteins; C100415:DSK2 protein, S cerevisiae; D011506:Proteins; C490845:RHP23 protein, S pombe; C122019:RPN10 protein, S cerevisiae; C086926:SIC1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D029702:Schizosaccharomyces pombe Proteins; D014452:Ubiquitins; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease