The destruction box of the cyclin Clb2 binds the anaphase-promoting complex/cyclosome subunit Cdc23.
Properly regulated cyclin proteolysis is critical for normal cell cycle progression. A nine-amino acid peptide motif called the destruction box (D box) is present at the N terminus of the yeast mitotic cyclins. This short sequence is required for cyclin ubiquitination and subsequent proteolysis. The anaphase-promoting complex/cyclosome (APC/C) is a ... multisubunit E3 required for cyclin ubiquitination. We have tested the D box of five mitotic cyclins for interaction with six APC/C subunits. The APC/C subunit Cdc23, but not five other subunits tested, interacted by two-hybrid analysis with the N terminus of wild-type Clb2. None of these subunits interacted with the N termini of the cyclins Clb1, Clb3, or Clb5. Mutations in the D box sequences of Clb2 inhibited interaction with Cdc23 both in vivo and in vitro. Our results provide the first evidence for a direct interaction between an APC/C substrate (Clb2) and an APC/C subunit (Cdc23).
Mesh Terms:
Amino Acid Motifs, Binding Sites, Cell Cycle Proteins, Cyclin B, Fungal Proteins, Ligases, Mutation, Protein Binding, Protein Subunits, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Ubiquitin-Protein Ligase Complexes
Amino Acid Motifs, Binding Sites, Cell Cycle Proteins, Cyclin B, Fungal Proteins, Ligases, Mutation, Protein Binding, Protein Subunits, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques, Ubiquitin-Protein Ligase Complexes
Arch. Biochem. Biophys.
Date: Nov. 15, 2002
PubMed ID: 12413490
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