ArticleBiochimica et biophysica acta2012
Ascending the nucleosome face: recognition and function of structured domains in the histone H2A-H2B dimer.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- H2BE113K mutation promotes breast cancer metastasis through modulating chromatin dynamics.Science advances · 2026Article
- DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024Review
- Structural basis for nucleosome binding and catalysis by the yeast Rpd3S/HDAC holoenzyme.Cell research · 2023Article
- Replication fork stalling elicits chromatin compaction for the stability of stalling replication forks.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Effects of histone H2B ubiquitylation on the nucleosome structure and dynamics.Nucleic acids research · 2018Article
- A cassette of basic amino acids in histone H2B regulates nucleosome dynamics and access to DNA damage.The Journal of biological chemistry · 2018Article
- Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding inGenetics · 2017Article
- A basic domain in the histone H2B N-terminal tail is important for nucleosome assembly by FACT.Nucleic acids research · 2016Article
- The Nucleosome Acidic Patch Regulates the H2B K123 Monoubiquitylation Cascade and Transcription Elongation in Saccharomyces cerevisiae.PLoS genetics · 2015Article
- Histone chaperone Anp32e removes H2A.Z from DNA double-strand breaks and promotes nucleosome reorganization and DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- FACT and the H2B N tail.Molecular and cellular biology · 2014Article
- A highly conserved region within H2B is important for FACT to act on nucleosomes.Molecular and cellular biology · 2014Article
- The variant histone H2A.V of Drosophila--three roles, two guises.Chromosoma · 2013Review
- Histone H2A variants in nucleosomes and chromatin: more or less stable?Nucleic acids research · 2012Review
- Chromatin modification by PSC occurs at one PSC per nucleosome and does not require the acidic patch of histone H2A.PloS one · 2012Article
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Authors and funding
3 authors.
Funding
Abstract
Research over the past decade has greatly expanded our understanding of the nucleosome's role as a dynamic hub that is specifically recognized by many regulatory proteins involved in transcription, silencing, replication, repair, and chromosome segregation. While many of these nucleosome interactions are mediated by post-translational modifications in the disordered histone tails, it is becoming increasingly apparent that structured regions of the nucleosome, including the histone fold domains, are also recognized by numerous regulatory proteins. This review will focus on the recognition of structured domains in the histone H2A-H2B dimer, including the acidic patch, the H2A docking domain, the H2B α3-αC helices, and the HAR/HBR domains, and will survey the known biological functions of histone residues within these domains. Novel post-translational modifications and trans-histone regulatory pathways involving structured regions of the H2A-H2B dimer will be highlighted, along with the role of intrinsic disorder in the recognition of structured nucleosome regions.
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