ArticleNucleic acids research2007
Cooperative binding of the yeast Spt10p activator to the histone upstream activating sequences is mediated through an N-terminal dimerization domain.
Article in Nucleic acids research, 2007. 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, 12 citations in OpenAlex.
- Multilevel Regulation of Membrane Proteins in Response to Metal and Metalloid Stress: A Lesson from Yeast.International journal of molecular sciences · 2024Review
- The Spt10 GNAT Superfamily Protein Modulates Development, Cell Cycle Progression and Virulence in the Fungal Insect Pathogen,Journal of fungi (Basel, Switzerland) · 2021Article
- Characterisation of functional domains in fission yeast Ams2 that are required for core histone gene transcription.Scientific reports · 2016Article
- Regulation of cell-to-cell variability in divergent gene expression.Nature communications · 2016Article
- Cell cycle-regulated oscillator coordinates core histone gene transcription through histone acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Cell-cycle perturbations suppress the slow-growth defect of spt10Δ mutants in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2013Article
- Regulation of histone gene expression in budding yeast.Genetics · 2012Review
- Spt10 and Swi4 control the timing of histone H2A/H2B gene activation in budding yeast.Molecular and cellular biology · 2011Article
- Spt10 and Spt21 are required for transcriptional silencing in Saccharomyces cerevisiae.Eukaryotic cell · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The yeast Spt10p activator is a putative histone acetyltransferase (HAT) possessing a sequence-specific DNA-binding domain (DBD) which binds to the upstream activation sequences (UAS elements) in the histone gene promoters. Spt10p binds to a pair of histone UAS elements with extreme positive cooperativity. The molecular basis of this cooperativity was addressed. Spt10p (640 residues) is an elongated dimer, but the isolated DBD (residues 283-396) is a monomer and binds non-cooperatively to DNA. A Spt10p fragment comprising the N-terminal domain (NTD), HAT domain and DBD (residues 1-396) binds cooperatively and is a dimer, whereas an overlapping Spt10p fragment comprising the DBD and C-terminal domains (residues 283-640) binds non-cooperatively and is a monomer. These observations imply that cooperative binding requires dimerization. The isolated NTD (residues 1-98) is a dimer and is responsible for dimerization. We propose that cooperativity involves a conformational change in the Spt10p dimer which facilitates the simultaneous recognition of two UAS elements. In vivo, deletion of the NTD results in poor growth, but does not prevent the binding at the HTA1 promoter, suggesting that dimerization is biologically important. Residues 1-396 are sufficient for normal growth, indicating that the critical functions of Spt10p reside in the N-terminal domains.
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