Genomes and Genes
Gene Symbol: His2A:CG31618
Description: histone H2A
Alias: BEST:CK01438, CG31618, Dmel\CG31618, histone H2A, CG31618-PA, His2A:CG31618-PA
Species: fruit fly
- Clapier C, Chakravarthy S, Petosa C, Fernández Tornero C, Luger K, Müller C. Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. Proteins. 2008;71:1-7 pubmed..This highlights the tight evolutionary constraints exerted on histones since the vertebrate and invertebrate lineages diverged. ..
- Kusch T, Mei A, Nguyen C. Histone H3 lysine 4 trimethylation regulates cotranscriptional H2A variant exchange by Tip60 complexes to maximize gene expression. Proc Natl Acad Sci U S A. 2014;111:4850-5 pubmed publisher..Furthermore, this mechanism prevents the accumulation of epigenetic noise caused by random complex-nucleosome collisions. ..
- Klinker H, Haas C, Harrer N, Becker P, Mueller Planitz F. Rapid purification of recombinant histones. PLoS ONE. 2014;9:e104029 pubmed publisher..We expect that the RHP protocol can be readily applied to the purification of canonical histones from other species as well as the numerous histone variants. ..
- Carrier F, Georgel P, Pourquier P, Blake M, Kontny H, Antinore M, et al. Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin. Mol Cell Biol. 1999;19:1673-85 pubmed..Both histone acetylation and UV radiation are thought to destabilize the nucleosomal structure. Hence, these results imply that Gadd45 can recognize an altered chromatin state and modulate DNA accessibility to cellular proteins. ..
- Lagarou A, Mohd Sarip A, Moshkin Y, Chalkley G, Bezstarosti K, Demmers J, et al. dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing. Genes Dev. 2008;22:2799-810 pubmed publisher..Here, we describe a novel mode of histone crosstalk during gene silencing, in which histone H2A monoubiquitylation is coupled to the removal of histone H3 Lys 36 dimethylation (H3K36me2)...
- Zhou B, Feng H, Ghirlando R, Li S, Schwieters C, Bai Y. A Small Number of Residues Can Determine if Linker Histones Are Bound On or Off Dyad in the Chromatosome. J Mol Biol. 2016;428:3948-3959 pubmed publisher..Taken together, our results suggest that a small number of residues in the globular domain of a linker histone can control its binding location on the nucleosome and higher-order chromatin structure. ..