Histone H2B type 2-E is a protein that in humans is encoded by the HIST2H2BEgene.[3][4][5]
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene encodes a member of the histone H2B family, and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif.[5]
HIST2H2BE gene has been detected progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy.[6] For this reason, this gene is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.[6]
^ abRotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. PMID25205602. S2CID24986454.
Further reading[]
Collart D, Ramsey-Ewing A, Bortell R, et al. (1991). "Isolation and characterization of a cDNA from a human histone H2B gene which is reciprocally expressed in relation to replication-dependent H2B histone genes during HL60 cell differentiation". Biochemistry. 30 (6): 1610–7. doi:10.1021/bi00220a024. PMID1993178.
Jackson S, Brooks W, Jackson V (1994). "Dynamics of the interactions of histones H2A,H2B and H3,H4 with torsionally stressed DNA". Biochemistry. 33 (18): 5392–403. doi:10.1021/bi00184a006. PMID8180162.
Rodriguez P, Munroe D, Prawitt D, et al. (1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". Genomics. 44 (3): 253–65. doi:10.1006/geno.1997.4868. PMID9325046.
Freire J, Covelo G, Sarandeses C, et al. (2001). "Identification of nuclear-import and cell-cycle regulatory proteins that bind to prothymosin alpha". Biochem. Cell Biol. 79 (2): 123–31. doi:10.1139/bcb-79-2-123. PMID11310559.
Nemergut ME, Mizzen CA, Stukenberg T, et al. (2001). "Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B". Science. 292 (5521): 1540–3. Bibcode:2001Sci...292.1540N. doi:10.1126/science.292.5521.1540. PMID11375490.