ArticleMolecular and cellular biology1997
Sin mutations of histone H3: influence on nucleosome core structure and function.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 76 citations in OpenAlex.
- Histone Modifications in the Cell Cycle ofEpigenomes · 2026Review
- Cryo-EM structure and biochemical analyses of the nucleosome containing the cancer-associated histone H3 mutation E97K.Genes to cells : devoted to molecular & cellular mechanisms · 2024Article
- Histone mutations in cancer.Biochemical Society transactions · 2023Article
- Review
- Micromechanical Study of Hyperacetylated Nucleosomes Using Single Molecule Transverse Magnetic Tweezers.International journal of molecular sciences · 2023Article
- Reb1, Cbf1, and Pho4 Bias Histone Sliding and Deposition Away from Their Binding Sites.Molecular and cellular biology · 2022Article
- Unusual nucleosome formation and transcriptome influence by the histone H3mm18 variant.Nucleic acids research · 2022Article
- Structural studies of functional nucleosome complexes with transacting factors.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022Review
- Structural rearrangements of the histone octamer translocate DNA.Nature communications · 2018Article
- Plasmodium falciparum Nucleosomes Exhibit Reduced Stability and Lost Sequence Dependent Nucleosome Positioning.PLoS pathogens · 2016Article
- Histone H3.5 forms an unstable nucleosome and accumulates around transcription start sites in human testis.Epigenetics & chromatin · 2016Article
- Histone Acetylation near the Nucleosome Dyad Axis Enhances Nucleosome Disassembly by RSC and SWI/SNF.Molecular and cellular biology · 2015Article
- Histone Sprocket Arginine Residues Are Important for Gene Expression, DNA Repair, and Cell Viability in Saccharomyces cerevisiae.Genetics · 2015Article
- Arginine-phosphate salt bridges between histones and DNA: intermolecular actuators that control nucleosome architecture.The Journal of chemical physics · 2014Article
- Scratching the (lateral) surface of chromatin regulation by histone modifications.Nature structural & molecular biology · 2013Article
- Unwinding and rewinding the nucleosome inner turn: force dependence of the kinetic rate constants.Physical review. E, Statistical, nonlinear, and soft matter physics · 2013Article
- Contribution of histone N-terminal tails to the structure and stability of nucleosomes.FEBS open bio · 2013Article
- Kinetics and thermodynamics of phenotype: unwinding and rewinding the nucleosome.Journal of molecular biology · 2012Article
- Regulation of the nucleosome unwrapping rate controls DNA accessibility.Nucleic acids research · 2012Article
- Identification of histone mutants that are defective for transcription-coupled nucleosome occupancy.Molecular and cellular biology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sin mutations in Saccharomyces cerevisiae alleviate transcriptional defects that result from the inactivation of the yeast SWVI/SNF complex. We have investigated the structural and functional consequences for the nucleosome of Sin mutations in histone H3. We directly test the hypothesis that mutations in histone H3 leading to a SWI/SNF-independent (Sin) phenotype in yeast lead to nucleosomal destabilization. In certain instances this is shown to be true; however, nucleosomal destabilization does not always occur. Topoisomerase I-mediated relaxation of minichromosomes assembled with either mutant histone H3 or wild-type H3 together with histones H2A, H2B, and H4 indicates that DNA is constrained into nucleosomal structures containing either mutant or wild-type proteins. However, nucleosomes containing particular mutant H3 molecules (R116-H and T118-I) are more accessible to digestion by micrococcal nuclease and do not constrain DNA in a precise rotational position, as revealed by digestion with DNase I. This result establishes that Sin mutations in histone H3 located close to the dyad axis can destabilize histone-DNA contacts at the periphery of the nucleosome core. Other nucleosomes containing a distinct mutant H3 molecule (E105-K) associated with a Sin phenotype show very little change in nucleosome structure and stability compared to wild-type nucleosomes. Both mutant and wild-type nucleosomes continue to restrict the binding of either TATA-binding protein/transcription factor IIA (TFIIA) or the RNA polymerase III transcription machinery. Thus, different Sin mutations in histone H3 alter the stability of histone-DNA interactions to various extents in the nucleosome while maintaining the fundamental architecture of the nucleosome and contributing to a common Sin phenotype.
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