{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Histone H3C13—one member of the canonical histone H3 family (e.g. encoded by genes such as HIST2H3C)—is emerging as a critical regulator of chromatin structure and function. Its incorporation into nucleosomes is central to the maintenance of genomic integrity, as it participates in DNA packaging during replication, repair, and differentiation. Post‐translational modifications (PTMs) of H3—including site‐specific acetylation (such as H3K56ac) that facilitates chromatin assembly following DNA damage and replication—underpin its role in coupling DNA synthesis with epigenetic control, with aberrant levels noted in cancer cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Furthermore, mutations affecting key residues in histone H3—including a novel K27M substitution in HIST2H3C—have been directly linked to aggressive pediatric tumors like diffuse intrinsic pontine glioma; such alterations perturb normal H3K27-trimethylation and thereby drive distinct oncogenic programs."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " In parallel, proteolytic events and other PTMs of H3 modulate its functions during cellular differentiation and stress responses"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": ", while its dynamic deposition is mediated by a suite of histone chaperones and chromatin-remodeling factors that ensure proper nucleosome assembly and epigenome maintenance."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " Collectively, these studies underscore that H3C13 functions not only as a structural component of chromatin but also as an integrator of diverse regulatory signals—through its PTMs and variant-specific dynamics—that modulate gene expression, cell cycle progression, and ultimately, cellular homeostasis and disease.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Chandrima Das, M Scott Lucia, Kirk C Hansen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CBP/p300-mediated acetylation of histone H3 on lysine 56."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature07861"}], "href": "https://doi.org/10.1038/nature07861"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19270680"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19270680"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "David Castel, Cathy Philippe, Raphaël Calmon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Histone H3F3A and HIST1H3B K27M mutations define two subgroups of diffuse intrinsic pontine gliomas with different prognosis and phenotypes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Acta Neuropathol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00401-015-1478-0"}], "href": "https://doi.org/10.1007/s00401-015-1478-0"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26399631"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26399631"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Elizabeth M Duncan, Tara L Muratore-Schroeder, Richard G Cook, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2008.09.055"}], "href": "https://doi.org/10.1016/j.cell.2008.09.055"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18957203"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18957203"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Hongda Huang, Caroline B Strømme, Giulia Saredi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb.3055"}], "href": "https://doi.org/10.1038/nsmb.3055"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26167883"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26167883"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Nikolay A Pchelintsev, Tony McBryan, Taranjit Singh Rai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Placing the HIRA histone chaperone complex in the chromatin landscape."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.celrep.2013.03.026"}], "href": "https://doi.org/10.1016/j.celrep.2013.03.026"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23602572"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23602572"}]}]}]}