Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-39328
Biochemistry 2005 Feb 22;447:2529-35. doi: 10.1021/bi048061n.
Show Gene links Show Anatomy links

Characterization of nucleosomes consisting of the human testis/sperm-specific histone H2B variant (hTSH2B).

Li A , Maffey AH , Abbott WD , Conde e Silva N , Prunell A , Siino J , Churikov D , Zalensky AO , AusiĆ³ J .


???displayArticle.abstract???
We have reported earlier the occurrence of a specific histone H2B variant in human testis and sperm. Here we have structurally characterized this protein, its association with the rest of the histone octamer, and its effects on the nucleosome structure. We show that a reconstituted octamer consisting of hTSH2B and a stoichiometric complement of histones H2A, H3, and H4 exhibits a lower stability compared to the reconstituted native counterpart consisting of H2B. In contrast, the hTSH2B containing octamers are able to form nucleosome core particles which are structurally and dynamically indistinguishable from those reconstituted with octamers consisting of only native histones. Furthermore, the presence of hTSH2B in the nucleosome does not affect its ability to bind to linker histones.

???displayArticle.pubmedLink??? 15709765
???displayArticle.link??? Biochemistry
???displayArticle.grants??? [+]

Genes referenced: h2a