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Histone H2A-Bbd type 2/3

Definition:

Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis.

References:

[1]. Yunhe Bao, et al. Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA. EMBO J. 2004 Aug 18;23(16):3314-24. [Content Brief]

[2]. Cécile-Marie Doyen, et al. Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome. EMBO J. 2006 Sep 20;25(18):4234-44. [Content Brief]

[3]. Rodrigo González-Romero, et al. Quickly evolving histones, nucleosome stability and chromatin folding: all about histone H2A.Bbd. Gene. 2008 Apr 30;413(1-2):1-7. [Content Brief]

[4]. Michael Y Tolstorukov, et al. Histone variant H2A.Bbd is associated with active transcription and mRNA processing in human cells. Mol Cell. 2012 Aug 24;47(4):596-607. [Content Brief]

[5]. Mitsuru Okuwaki, et al. Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I. Mol Cell Biol. 2005 Dec;25(23):10639-51. [Content Brief]

[6]. Hervé Menoni, et al. ATP-dependent chromatin remodeling is required for base excision repair in conventional but not in variant H2A.Bbd nucleosomes. Mol Cell Biol. 2007 Sep;27(17):5949-56. [Content Brief]

[7]. José María Eirín-López, et al. H2A.Bbd: a quickly evolving hypervariable mammalian histone that destabilizes nucleosomes in an acetylation-independent way. FASEB J. 2008 Jan;22(1):316-26. [Content Brief]

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