Abstract
The UBA domain is a motif found in a variety of proteins, some of which are associated with the ubiquitin-proteasome system. We describe the isolation of a fission-yeast gene, mud1+, which encodes a UBA domain containing protein that is able to bind multi-ubiquitin chains. We show that the UBA domain is responsible for this activity. Two other proteins containing this motif, the fission-yeast homologues of Rad23 and Dsk2, are also shown to bind multi-ubiquitin chains via their UBA domains. These two proteins are implicated, along with the fission-yeast Pus1(S5a/Rpn10) subunit of the 26 S proteasome, in the recognition and turnover of substrates by this proteolytic complex.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Cell Cycle Proteins / metabolism
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Cysteine Endopeptidases / metabolism
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DNA-Binding Proteins / metabolism
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Genes, Fungal
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Genes, Reporter / genetics
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Multienzyme Complexes / metabolism
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Phenotype
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Proteasome Endopeptidase Complex
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Protein Binding
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae Proteins*
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Schizosaccharomyces / chemistry*
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Schizosaccharomyces / genetics
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Schizosaccharomyces / physiology
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Schizosaccharomyces pombe Proteins*
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Surface Plasmon Resonance
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Ubiquitin / metabolism*
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Ubiquitins / metabolism
Substances
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Cell Cycle Proteins
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DNA-Binding Proteins
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DSK2 protein, S cerevisiae
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Fungal Proteins
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Multienzyme Complexes
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RAD23 protein, S cerevisiae
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RHP23 protein, S pombe
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Schizosaccharomyces pombe Proteins
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Ubiquitin
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Ubiquitins
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex