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H2A histone family, member B2

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene encodes a member of the histone H2A family. This gene is part of a region that is repeated three times on chromosome X, once in intron 22 of the F8 gene and twice closer to the Xq telomere. This record represents the middle copy. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: H2A, Histone, CAN, H1, SWI
Papers on H2A.Bbd
The histone variant H2A.Bbd is enriched at sites of DNA synthesis.
Imhof et al., München, Germany. In Nucleic Acids Res, 2014
H2A.Bbd and H2A revealed a strikingly different protein composition.
Localization and expression of histone H2A variants during mouse oogenesis and preimplantation embryo development.
Liu et al., Nanjing, China. In Genet Mol Res, 2013
We examined global localization and expression of the histone H2A variants, including H2A.Bbd, H2A.Z and H2A.X, during mouse oogenesis and preimplantation embryo development.
Histone variant selectivity at the transcription start site: H2A.Z or H2A.Lap1.
Tremethick et al., Canberra, Australia. In Nucleus, 2013
For example, during mouse spermatogenesis we found that the mouse homolog of human H2A.Bbd, H2A.Lap1, is targeted to the TSS of active genes expressed during specific stages of spermatogenesis.
Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that transiently associates with reorganized chromatin.
Kurumizaka et al., Tokyo, Japan. In Sci Rep, 2012
Human histone H2A.B (formerly H2A.Bbd), a non-allelic H2A variant, exchanges rapidly as compared to canonical H2A, and preferentially associates with actively transcribed genes.
Histone variant H2A.Bbd is associated with active transcription and mRNA processing in human cells.
Park et al., Boston, United States. In Mol Cell, 2012
Here we focus on H2A.Bbd, a rapidly evolving variant found in mammals but not in invertebrates.
Distinct distribution of ectopically expressed histone variants H2A.Bbd and MacroH2A in open and closed chromatin domains.
Razin et al., Moscow, Russia. In Plos One, 2011
Among the known histone variants the less characterized are H2A.Bbd and different forms of macroH2A.
The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling.
Dimitrov et al., Grenoble, France. In Nucleic Acids Res, 2011
Deletion of this domain or replacement with the incomplete docking domain from the variant H2A.Bbd results in significant structural alterations in the nucleosome, including an increase in overall accessibility to nucleases, un-wrapping of ∼10 bp of DNA from each end of the nucleosome and associated changes in the entry/exit angle of DNA ends.
H2A.Bbd: an X-chromosome-encoded histone involved in mammalian spermiogenesis.
Ausió et al., Victoria, Canada. In Nucleic Acids Res, 2010
Despite the identification of H2A.Bbd as a new vertebrate-specific replacement histone variant several years ago, and despite the many in vitro structural characterizations using reconstituted chromatin complexes consisting of this variant, the existence of H2A.Bbd in the cell and its location has remained elusive.
Characterisation of histone variant distribution in human embryonic stem cells by transfection of in vitro transcribed mRNA.
Saffery et al., Melbourne, Australia. In Mol Reprod Dev, 2009
The subcellular localisations of variant histone H3 (CENP-A, H3.3), H2A (MACROH2A, H2AX, H2AZ, H2ABBD) and H1 (H1A, HB, H1C, H1D) were examined, revealing distinct nuclear localisation profiles for each protein.
The dynamics of individual nucleosomes controls the chromatin condensation pathway: direct atomic force microscopy visualization of variant chromatin.
Faivre-Moskalenko et al., Lyon, France. In Biophys J, 2009
We show that a subtle modification in the nucleosome structure induced by the histone variant H2A.Bbd drastically modifies the higher order organization of the nucleosomal arrays.
Two novel mouse genes mapped to chromosome Yp are expressed specifically in spermatids.
Affara et al., Cambridge, United Kingdom. In Mamm Genome, 2009
A phylogenetic analysis of H2al genes together with other H2A genes indicates that H2al is most closely related to the mammalian-specific H2A.Bbd family of histones.
Quickly evolving histones, nucleosome stability and chromatin folding: all about histone H2A.Bbd.
Eirín-López et al., A Coruña, Spain. In Gene, 2008
Histone H2A.Bbd (Barr body-deficient) is a novel histone variant which is largely excluded from the inactive X chromosome of mammals.
H2A.Bbd: a quickly evolving hypervariable mammalian histone that destabilizes nucleosomes in an acetylation-independent way.
Ausió et al., Victoria, Canada. In Faseb J, 2008
Molecular evolutionary analyses revealed that histone H2A.Bbd is a highly variable quickly evolving mammalian replacement histone variant, in striking contrast to all other histones.
The nucleosome surface regulates chromatin compaction and couples it with transcriptional repression.
Tremethick et al., Canberra, Australia. In Nat Struct Mol Biol, 2007
This structure-function relationship has been exploited by complex eukaryotic cells through the replacement of H2A with the specific variant H2A.Bbd, which naturally lacks an acidic patch.
Histone variants--the structure behind the function.
Ausió, Victoria, Canada. In Brief Funct Genomic Proteomic, 2006
In this review, I am going to discuss several of the most recent structural studies on core histone (H2A.Bbd, H2A.Z, H2A.X, macroH2A, H3.3, CENP-A) and linker histone variants (histone H1 microheterogeneity) focusing on their role in nucleosome stability and chromatin fibre dynamics with special emphasis on their possible functional implications.
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