Format

Send to

Choose Destination
See comment in PubMed Commons below
Biophys J. 2014 May 20;106(10):2206-13. doi: 10.1016/j.bpj.2014.04.007.

Distinct features of the histone core structure in nucleosomes containing the histone H2A.B variant.

Author information

1
Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan. Electronic address: sugiyama@rri.kyoto-u.ac.jp.
2
(‡)Laboratory of Structural Biology, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan.
3
Research Reactor Institute, Kyoto University, Kumatori, Osaka 590-0494, Japan.
4
Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama 230-0045, Japan.
5
ISIS Facility, STFC Rutherford Appleton Laboratory, Didcot, OX11 0QX, UK.
6
(‡)Laboratory of Structural Biology, Waseda University, Shinjuku-ku, Tokyo 162-8480, Japan. Electronic address: kurumizaka@waseda.jp.

Abstract

Nucleosomes containing a human histone variant, H2A.B, in an aqueous solution were analyzed by small-angle neutron scattering utilizing a contrast variation technique. Comparisons with the canonical H2A nucleosome structure revealed that the DNA termini of the H2A.B nucleosome are detached from the histone core surface, and flexibly expanded toward the solvent. In contrast, the histone tails are compacted in H2A.B nucleosomes compared to those in canonical H2A nucleosomes, suggesting that they bind to the surface of the histone core and/or DNA. Therefore, the histone tail dynamics may function to regulate the flexibility of the DNA termini in the nucleosomes.

PMID:
24853749
PMCID:
PMC4052288
DOI:
10.1016/j.bpj.2014.04.007
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center