期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 503, 期 3, 页码 1786-1791出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2018.07.114
关键词
Histone variant; H2A.Bbd; Crystal structure
资金
- Chinese Ministry of Science and Technology [2015CB856200]
- Natural Science Foundation of China [31521002, 31671344]
- Strategic Priority Research Program [XDB08010104]
H2A.Bbd, the most divergent histone variant among all known H2A type histones, is involved in gene transcription, spermiogenesis, DNA replication and RNA splicing. Incorporation of H2A.Bbd-H2B dimer, a fundamental unit of H2A.Bbd nucleosome, modulate structures of nucleosome or chromatin, but the underlying mechanism remains elusive. Here we determined a crystal structure of H2A.Bbd-H2B dimer at 2.6 angstrom resolution. Although the H2A.Bbd-H2B dimer structure largely resembles that of H2A-H2B, substitution of H2A citC helix residues by H2A.Bbd counterparts lead to the transition of a long alpha C-helix to the short 3(10)-helix, likely owing to the rearrangement of the hydrogen-bond network. Moreover, structural comparison revealed a strikingly altered electrostatic potential surface for H2A.Bbd-H2B dimer displaying a diminished DNA binding capability. Our study provides the first high-resolution structure of histone variant H2A.Bbd and shed a light on biological function of H2A.Bbd. (C) 2018 Elsevier Inc. All rights reserved.
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