ArticleProceedings of the National Academy of Sciences of the United States of America2013
Heterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 citing papers in PubMed, 67 citations in OpenAlex.
- Physical interactions within the SIR heterochromatin complex potentiate inter-subunit communication and gene repression.Cell reports · 2026Article
- Epigenetic regulation of intracellular branched-chain amino acid homeostasis maintains a normal lifespan.iScience · 2025Article
- Transcriptional silencing in Saccharomyces cerevisiae: known unknowns.Epigenetics & chromatin · 2024Review
- Two-way feedback between chromatin compaction and histone modification state explainsProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Two-way feedback between chromatin compaction and histone modification state explainsbioRxiv : the preprint server for biology · 2023Article
- The regional sequestration of heterochromatin structural proteins is critical to form and maintain silent chromatin.Epigenetics & chromatin · 2022Review
- Article
- Distinct structural groups of histone H3 and H4 residues have divergent effects on chronological lifespan in Saccharomyces cerevisiae.PloS one · 2022Article
- Measuring the buffering capacity of gene silencing inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Coupling of H3K27me3 recognition with transcriptional repression through the BAH-PHD-CPL2 complex in Arabidopsis.Nature communications · 2020Article
- Therapeutic strategies against hDOT1L as a potential drug target in MLL-rearranged leukemias.Clinical epigenetics · 2020Review
- Structure and function of the Orc1 BAH-nucleosome complex.Nature communications · 2019Article
- Structural Basis of Dot1L Stimulation by Histone H2B Lysine 120 Ubiquitination.Molecular cell · 2019Article
- The EZH2 SANT1 domain is a histone reader providing sensitivity to the modification state of the H4 tail.Scientific reports · 2019Article
- Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4.Nature communications · 2019Article
- SIR proteins create compact heterochromatin fibers.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Expanding heterochromatin reveals discrete subtelomeric domains delimited by chromatin landscape transitions.Genome research · 2018Article
- The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin.Current genetics · 2018Review
- Cryo-EM of nucleosome core particle interactions in trans.Scientific reports · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The regulated binding of effector proteins to the nucleosome plays a central role in the activation and silencing of eukaryotic genes. How this binding changes the properties of chromatin to mediate gene activation or silencing is not fully understood. Here we provide evidence that association of the budding yeast silent information regulator 3 (Sir3) silencing protein with the nucleosome induces a conformational change in the amino terminus of histone H4 that promotes interactions between the conserved H4 arginines 17 and 19 (R17 and R19) and nucleosomal DNA. Substitutions of H4R17 and R19 with alanine abolish silencing in vivo, but have little or no effect on binding of Sir3 to nucleosomes or histone H4 peptides in vitro. Furthermore, in both the previously reported crystal structure of the Sir3-bromo adjacent homology (BAH) domain bound to the Xenopus laevis nucleosome core particle and the crystal structure of the Sir3-BAH domain bound to the yeast nucleosome core particle described here, H4R17 and R19 make contacts with nucleosomal DNA rather than with Sir3. These results suggest that Sir3 binding generates a more stable nucleosome by clamping H4R17 and R19 to nucleosomal DNA, and raise the possibility that such induced changes in histone-DNA contacts play major roles in the regulation of chromatin structure.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.