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==== Chromosome condensation ==== ; ''Phosphorylation of H3 at serine 10 (phospho-H3S10)'': The mitotic kinase [[aurora B]] phosphorylates histone H3 at serine 10, triggering a cascade of changes that mediate mitotic chromosome condensation.<ref>{{cite journal |vauthors=Wilkins BJ, Rall NA, Ostwal Y, Kruitwagen T, Hiragami-Hamada K, Winkler M, Barral Y, Fischle W, Neumann H |date=January 2014 |title=A cascade of histone modifications induces chromatin condensation in mitosis |url=https://www.science.org/doi/10.1126/science.1244508 |journal=Science |volume=343 |issue=6166 |pages=77–80 |bibcode=2014Sci...343...77W |doi=10.1126/science.1244508 |pmid=24385627 |hdl-access=free |s2cid=7698266 |hdl=11858/00-001M-0000-0015-11C0-5}}</ref><ref>{{cite journal |vauthors=Johansen KM, Johansen J |date=2006 |title=Regulation of chromatin structure by histone H3S10 phosphorylation |url=https://link.springer.com/article/10.1007/s10577-006-1063-4 |journal=Chromosome Research |volume=14 |issue=4 |pages=393–404 |doi=10.1007/s10577-006-1063-4 |pmid=16821135 |s2cid=8556959}}</ref> Condensed chromosomes therefore stain very strongly for this mark, but H3S10 phosphorylation is also present at certain chromosome sites outside mitosis, for example in pericentric heterochromatin of cells during G2. H3S10 phosphorylation has also been linked to DNA damage caused by [[R-loop]] formation at highly transcribed sites.<ref>{{cite journal | vauthors = Castellano-Pozo M, Santos-Pereira JM, Rondón AG, Barroso S, Andújar E, Pérez-Alegre M, García-Muse T, Aguilera A | title = R loops are linked to histone H3 S10 phosphorylation and chromatin condensation | journal = Molecular Cell | volume = 52 | issue = 4 | pages = 583–90 | date = November 2013 | pmid = 24211264 | doi = 10.1016/j.molcel.2013.10.006 | doi-access = free }}</ref> ;''Phosphorylation H2B at serine 10/14 (phospho-H2BS10/14)'': Phosphorylation of H2B at serine 10 (yeast) or serine 14 (mammals) is also linked to chromatin condensation, but for the very different purpose of mediating chromosome condensation during apoptosis.<ref>{{cite journal | vauthors = Cheung WL, Ajiro K, Samejima K, Kloc M, Cheung P, Mizzen CA, Beeser A, Etkin LD, Chernoff J, Earnshaw WC, Allis CD | title = Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase | journal = Cell | volume = 113 | issue = 4 | pages = 507–17 | date = May 2003 | pmid = 12757711 | doi = 10.1016/s0092-8674(03)00355-6 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Ahn SH, Cheung WL, Hsu JY, Diaz RL, Smith MM, Allis CD | title = Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae | journal = Cell | volume = 120 | issue = 1 | pages = 25–36 | date = January 2005 | pmid = 15652479 | doi = 10.1016/j.cell.2004.11.016 | doi-access = free }}</ref> This mark is not simply a late acting bystander in apoptosis as yeast carrying mutations of this residue are resistant to hydrogen peroxide-induced apoptotic cell death.
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