Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.
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Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins. / Seeger, Michael; Hartmann-Petersen, Rasmus; Wilkinson, Caroline R M; Wallace, Mairi; Samejima, Itaru; Taylor, Martin S; Gordon, Colin.
In: Journal of Biological Chemistry, Vol. 278, No. 19, 2003, p. 16791-6.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.
AU - Seeger, Michael
AU - Hartmann-Petersen, Rasmus
AU - Wilkinson, Caroline R M
AU - Wallace, Mairi
AU - Samejima, Itaru
AU - Taylor, Martin S
AU - Gordon, Colin
N1 - 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
PY - 2003
Y1 - 2003
N2 - 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.
AB - 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.
U2 - 10.1074/jbc.M208281200
DO - 10.1074/jbc.M208281200
M3 - Journal article
C2 - 12615927
VL - 278
SP - 16791
EP - 16796
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 19
ER -
ID: 6493239