HIST1H2BF

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 large histone gene cluster on chromosome 6.^[3]

References

^ Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (Apr 1997). "Human histone gene organization: nonregular arrangement within a large cluster". Genomics 40 (2): 314–22. doi:10.1006/geno.1996.4592. PMID 9119399.
^ 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: HIST1H2BF histone cluster 1, H2bf". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8343.

Ohe Y, Hayashi H, Iwai K (1979). "Human spleen histone H2B. Isolation and amino acid sequence". J. Biochem. 85 (2): 615–24. PMID 422550.
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.
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. PMC 110633. PMID 9566873. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110633.
Albig W, Trappe R, Kardalinou E, et al. (1999). "The human H2A and H2B histone gene complement". Biol. Chem. 380 (1): 7–18. doi:10.1515/BC.1999.002. PMID 10064132.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=291826.

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

HIST1H2BF

References

Further reading