ArticleMolecular biology of the cell2002
Repression and activation domains of RME1p structurally overlap, but differ in genetic requirements.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Destabilization of mRNAs enhances competence to initiate meiosis in mouse spermatogenic cells.Development (Cambridge, England) · 2024Article
- mNature communications · 2019Article
- Dominant Epistasis Between Two Quantitative Trait Loci Governing Sporulation Efficiency in YeastFood technology and biotechnology · 2015Article
- Article
- Review
- Switching the mechanism of mating type switching: a domesticated transposase supplants a domesticated homing endonuclease.Genes & development · 2010Article
- Different mating-type-regulated genes affect the DNA repair defects of Saccharomyces RAD51, RAD52 and RAD55 mutants.Genetics · 2006Article
- Article
- Three mating type-like loci in Candida glabrata.Eukaryotic cell · 2003Article
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Authors and funding
4 authors.
Funding
Abstract
Rme1p, a repressor of meiosis in the yeast Saccharomyces cerevisiae, acts as both a transcriptional repressor and activator. Rme1p is a zinc-finger protein with no other homology to any protein of known function. The C-terminal DNA binding domain of Rme1p is essential for function. We find that mutations and progressive deletions in all three zinc fingers can be rescued by fusion of RME1 to the DNA binding domain of another protein. Thus, structural integrity of the zinc fingers is not required for the Rme1p-mediated effects on transcription. Using a series of mutant Rme1 proteins, we have characterized domains responsible for repression and activation. We find that the minimal transcriptional repression and activation domains completely overlap and lie in an 88-amino-acid N-terminal segment (aa 61-148). An additional transcriptional effector determinant lies in the first 31 amino acids of the protein. Notwithstanding the complete overlap between repression and activation domains of Rme1p, we demonstrated a functional difference between repression and activation: Rgr1p and Sin4p are absolutely required for repression but dispensable for activation.
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