<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>8(1)</volume><submitter>Tan GS</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>The execution of meiotic nuclear divisions in S. cerevisiae is regulated by protein degradation mediated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase. The correct timing of APC/C activity is essential for normal chromosome segregation. During meiosis, the APC/C is activated by the association of either Cdc20p or the meiosis-specific factor Ama1p. Both Ama1p and Cdc20p are targeted for degradation as cells exit meiosis II with Cdc20p being destroyed by APC/CAma1. In this study we investigated how Ama1p is down regulated at the completion of meiosis.&lt;h4>Findings&lt;/h4>Here we show that Ama1p is a substrate of APC/CCdc20 but not APC/CCdh1 in meiotic cells. Cdc20p binds Ama1p in vivo and APC/CCdc20 ubiquitylates Ama1p in vitro. Ama1p ubiquitylation requ</pubmed_abstract><journal>Cell division</journal><pagination>9</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3734102</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Mutually dependent degradation of Ama1p and Cdc20p terminates APC/C ubiquitin ligase activity at the completion of meiotic development in yeast.</pubmed_title><pmcid>PMC3734102</pmcid><pubmed_authors>Cooper KF</pubmed_authors><pubmed_authors>Lewandowski R</pubmed_authors><pubmed_authors>Mallory MJ</pubmed_authors><pubmed_authors>Tan GS</pubmed_authors><pubmed_authors>Strich R</pubmed_authors></additional><is_claimable>false</is_claimable><name>Mutually dependent degradation of Ama1p and Cdc20p terminates APC/C ubiquitin ligase activity at the completion of meiotic development in yeast.</name><description>&lt;h4>Background&lt;/h4>The execution of meiotic nuclear divisions in S. cerevisiae is regulated by protein degradation mediated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase. The correct timing of APC/C activity is essential for normal chromosome segregation. During meiosis, the APC/C is activated by the association of either Cdc20p or the meiosis-specific factor Ama1p. Both Ama1p and Cdc20p are targeted for degradation as cells exit meiosis II with Cdc20p being destroyed by APC/CAma1. In this study we investigated how Ama1p is down regulated at the completion of meiosis.&lt;h4>Findings&lt;/h4>Here we show that Ama1p is a substrate of APC/CCdc20 but not APC/CCdh1 in meiotic cells. Cdc20p binds Ama1p in vivo and APC/CCdc20 ubiquitylates Ama1p in vitro. Ama1p ubiquitylation requ</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Jul</publication><modification>2025-06-01T01:50:57.348Z</modification><creation>2025-06-01T01:50:57.348Z</creation></dates><accession>S-EPMC3734102</accession><cross_references><pubmed>23816140</pubmed><doi>10.1186/1747-1028-8-9</doi></cross_references></HashMap>