| Literature DB >> 15709765 |
Andra Li1, Allison H Maffey, Wade D Abbott, Natalia Conde e Silva, Ariel Prunell, Joseph Siino, Dmitrii Churikov, Andrei O Zalensky, Juan Ausió.
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.Entities:
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Year: 2005 PMID： 15709765 DOI： 10.1021/bi048061n
Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162