Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Journal of Biological Chemistry |
Volume | 278 |
Issue number | 19 |
Pages (from-to) | 16791-6 |
Number of pages | 5 |
ISSN | 0021-9258 |
DOIs | |
Publication status | Published - 2003 |
Bibliographical note
Keywords: Amino Acid Sequence; Carrier Proteins; Cysteine Endopeptidases; DNA-Binding Proteins; Fungal Proteins; Hydro-Lyases; Ligases; Molecular Sequence Data; Multienzyme Complexes; Proteasome Endopeptidase Complex; Protein Binding; Schizosaccharomyces; Schizosaccharomyces pombe Proteins; Sequence Alignment; Ubiquitin-Protein Ligase Complexes
ID: 6493239