H2A.Bbd: an X-chromosome-encoded histone involved in mammalian spermiogenesis.
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.
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.
Histone variants--the structure behind the function.
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.