Abstract
Fission yeast Rhp23 and Pus1 represent two families of multiubiquitin chain-binding proteins that associate with the proteasome. We show that both proteins bind to different regions of the proteasome subunit Mts4. The binding site for Pus1 was mapped to a cluster of repetitive sequences also found in the proteasome subunit SpRpn2 and the anaphase-promoting complex/cyclosome (APC/C) subunit Cut4. The putative role of Pus1 as a factor involved in allocation of ubiquitinylated substrates for the proteasome is discussed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anaphase-Promoting Complex-Cyclosome
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Carrier Proteins / metabolism*
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Cysteine Endopeptidases / metabolism
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DNA-Binding Proteins / metabolism*
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Fungal Proteins / metabolism*
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Hydro-Lyases / metabolism*
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Intracellular Signaling Peptides and Proteins
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Ligases / metabolism*
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Molecular Sequence Data
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Multienzyme Complexes / metabolism
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Proteasome Endopeptidase Complex
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Protein Binding
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Schizosaccharomyces / metabolism
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Schizosaccharomyces pombe Proteins / metabolism*
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Sequence Alignment
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Ubiquitin-Protein Ligase Complexes*
Substances
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Carrier Proteins
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DNA-Binding Proteins
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Fungal Proteins
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Intracellular Signaling Peptides and Proteins
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MTS4 protein, S pombe
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Multienzyme Complexes
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RHP23 protein, S pombe
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Schizosaccharomyces pombe Proteins
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Ubiquitin-Protein Ligase Complexes
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Anaphase-Promoting Complex-Cyclosome
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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Hydro-Lyases
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pseudouridylate synthetase
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Ligases