Abstract
Proteolysis mediated by the anaphase-promoting complex (APC) triggers chromosome segregation and exit from mitosis, yet its regulation is poorly understood. The conserved Cdc20 and Cdh1 proteins were identified as limiting, substrate-specific activators of APC-dependent proteolysis. CDC20 was required for the degradation of the APC substrate Pds1 but not for that of other APC substrates, such as Clb2 and Ase1. Conversely, cdh1Delta mutants were impaired in the degradation of Ase1 and Clb2 but not in that of Pds1. Overexpression of either CDC20 or CDH1 was sufficient to induce APC-dependent proteolysis of the appropriate target in stages of the cell cycle in which substrates are normally stable.
MeSH terms
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Anaphase-Promoting Complex-Cyclosome
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Cdc20 Proteins
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / metabolism*
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Cyclin B*
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Cyclins / metabolism
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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G1 Phase
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Ligases / metabolism*
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Mitosis
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Mutation
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Nuclear Proteins / metabolism
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Open Reading Frames
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S Phase
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins*
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Securin
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Substrate Specificity
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Ubiquitin-Protein Ligase Complexes*
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Ubiquitin-Protein Ligases
Substances
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CDC20 protein, S cerevisiae
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CLB2 protein, S cerevisiae
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Cdc20 Proteins
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Cell Cycle Proteins
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Cyclin B
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Cyclins
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Fungal Proteins
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Nuclear Proteins
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PDS1 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Securin
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Ubiquitin-Protein Ligase Complexes
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Anaphase-Promoting Complex-Cyclosome
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Ubiquitin-Protein Ligases
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Ligases