Histone H2B type 1-O is a protein that in humans is encoded by the HIST1H2BO gene .[5] [6] [7]
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 is intronless and encodes a member of the histone H2B family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. This gene is found in the small histone gene cluster on chromosome 6p22-p21.3.[7]
References [ ]
^ a b c GRCh38: Ensembl release 89: ENSG00000274641 - Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000069308 - Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ Dobner T, Wolf I, Mai B, Lipp M (Feb 1992). "A novel divergently transcribed human histone H2A/H2B gene pair". DNA Seq . 1 (6): 409–13. doi :10.3109/10425179109020799 . PMID 1768865 . ^ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (Oct 2002). "The human and mouse replication-dependent histone genes". Genomics . 80 (5): 487–98. doi :10.1016/S0888-7543(02)96850-3 . PMID 12408966 . ^ a b "Entrez Gene: HIST1H2BO histone cluster 1, H2bo" .
Further reading [ ]
Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 locus". Hum. Genet . 101 (3): 284–94. doi :10.1007/s004390050630 . PMID 9439656 . S2CID 38539096 . El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional Activation of the Integrated Chromatin-Associated Human Immunodeficiency Virus Type 1 Promoter" . Mol. Cell. Biol . 18 (5): 2535–44. doi :10.1128/mcb.18.5.2535 . PMC 110633 PMID 9566873 . Deng L, de la Fuente C, Fu P, et al. (2001). "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones" . Virology . 277 (2): 278–95. doi :10.1006/viro.2000.0593 PMID 11080476 . Deng L, Wang D, de la Fuente C, et al. (2001). "Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA" . Virology . 289 (2): 312–26. doi :10.1006/viro.2001.1129 PMID 11689053 . Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences" . Proc. Natl. Acad. Sci. U.S.A . 99 (26): 16899–903. doi :10.1073/pnas.242603899 PMC 139241 PMID 12477932 . Cheung WL, Ajiro K, Samejima K, et al. (2003). "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase" . Cell . 113 (4): 507–17. doi :10.1016/S0092-8674(03)00355-6 PMID 12757711 . S2CID 21854 . Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6" . Nature . 425 (6960): 805–11. Bibcode :2003Natur.425..805M . doi :10.1038/nature02055 PMID 14574404 . Lusic M, Marcello A, Cereseto A, Giacca M (2004). "Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter" . EMBO J . 22 (24): 6550–61. doi :10.1093/emboj/cdg631 . PMC 291826 PMID 14657027 . Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)" . Genome Res . 14 (10B): 2121–7. doi :10.1101/gr.2596504 . PMC 528928 PMID 15489334 . Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature . 433 (7021): 77–83. Bibcode :2005Natur.433...77A . doi :10.1038/nature03207 . PMID 15635413 . S2CID 4344740 . Golebiowski F, Kasprzak KS (2007). "Inhibition of core histones acetylation by carcinogenic nickel(II)" . Mol. Cell. Biochem . 279 (1–2): 133–9. doi :10.1007/s11010-005-8285-1 . PMID 16283522 . S2CID 25071586 . Zhu B, Zheng Y, Pham AD, et al. (2006). "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation" . Mol. Cell . 20 (4): 601–11. doi :10.1016/j.molcel.2005.09.025 PMID 16307923 . Bonenfant D, Coulot M, Towbin H, et al. (2006). "Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry" . Mol. Cell. Proteomics . 5 (3): 541–52. doi :10.1074/mcp.M500288-MCP200 PMID 16319397 . Beck HC, Nielsen EC, Matthiesen R, et al. (2006). "Quantitative proteomic analysis of post-translational modifications of human histones" . Mol. Cell. Proteomics . 5 (7): 1314–25. doi :10.1074/mcp.M600007-MCP200 PMID 16627869 . Pavri R, Zhu B, Li G, et al. (2006). "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II" . Cell . 125 (4): 703–17. doi :10.1016/j.cell.2006.04.029 PMID 16713563 . S2CID 2614680 . Kim SC, Sprung R, Chen Y, et al. (2006). "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey" . Mol. Cell . 23 (4): 607–18. doi :10.1016/j.molcel.2006.06.026 PMID 16916647 .
PDB gallery
1aoi : COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
1eqz : X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION
1f66 : 2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z
1hq3 : CRYSTAL STRUCTURE OF THE HISTONE-CORE-OCTAMER IN KCL/PHOSPHATE
1kx3 : X-Ray Structure of the Nucleosome Core Particle, NCP146, at 2.0 A Resolution
1kx4 : X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution
1kx5 : X-Ray Structure of the Nucleosome Core Particle, NCP147, at 1.9 A Resolution
1m18 : LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
1m19 : LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
1m1a : LIGAND BINDING ALTERS THE STRUCTURE AND DYNAMICS OF NUCLEOSOMAL DNA
1p34 : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3a : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3b : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3f : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3g : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3i : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3k : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3l : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3m : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3o : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1p3p : Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants
1s32 : Molecular Recognition of the Nucleosomal 'Supergroove'
1tzy : Crystal Structure of the Core-Histone Octamer to 1.90 Angstrom Resolution
1u35 : Crystal structure of the nucleosome core particle containing the histone domain of macroH2A
1zbb : Structure of the 4_601_167 Tetranucleosome
1zla : X-ray Structure of a Kaposi's sarcoma herpesvirus LANA peptide bound to the nucleosomal core
2aro : Crystal Structure Of The Native Histone Octamer To 2.1 Angstrom Resolution, Crystalised In The Presence Of S-Nitrosoglutathione
2cv5 : Crystal structure of human nucleosome core particle
2f8n : 2.9 Angstrom X-ray structure of hybrid macroH2A nucleosomes
2fj7 : Crystal structure of Nucleosome Core Particle Containing a Poly (dA.dT) Sequence Element
2hio : HISTONE OCTAMER (CHICKEN), CHROMOSOMAL PROTEIN
2nzd : Nucleosome core particle containing 145 bp of DNA
