Gcn5p-dependent acetylation induces degradation of the meiotic transcriptional repressor Ume6p

Michael J. Mallory, Michael J. Law, David E. Sterner, Shelley L. Berger, Randy Strich

    Research output: Contribution to journalArticlepeer-review

    16 Scopus citations

    Abstract

    Ume6p represses early meiotic gene transcription in Saccharomyces cerevisiae by recruiting the Rpd3p histone deacetylase and chromatin-remodeling proteins. Ume6p repression is relieved in a two-step destruction process mediated by the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. The first step induces partial Ume6p degradation when vegetative cells shift from glucose- to acetate-based medium. Complete proteolysis happens only upon meiotic entry. Here we demonstrate that the first step in Ume6p destruction is controlled by its acetylation and deacetylation by the Gcn5p acetyltransferase and Rpd3p, respectively. Ume6p acetylation occurs in medium lacking dextrose and results in a partial destruction of the repressor. Preventing acetylation delays Ume6p meiotic destruction and retards both the transient transcription program and execution of the meiotic nuclear divisions. Conversely, mimicking acetylation induces partial destruction of Ume6p in dextrose medium and accelerates meiotic degradation by the APC/C. These studies reveal a new mechanism by which acetyltransferase activity induces gene expression through targeted destruction of a transcriptional repressor. These findings also demonstrate an important role for nonhistone acetylation in the transition between mitotic and meiotic cell division.

    Original languageEnglish (US)
    Pages (from-to)1609-1617
    Number of pages9
    JournalMolecular biology of the cell
    Volume23
    Issue number9
    DOIs
    StatePublished - May 1 2012

    All Science Journal Classification (ASJC) codes

    • Molecular Biology
    • Cell Biology

    Fingerprint

    Dive into the research topics of 'Gcn5p-dependent acetylation induces degradation of the meiotic transcriptional repressor Ume6p'. Together they form a unique fingerprint.

    Cite this