A Small Number of Residues Can Determine if Linker Histones Are Bound On or Off Dyad in the Chromatosome
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- 作者：Bing-Rui Zhou1 ; Hanqiao Feng1 ; Rodolfo Ghirlando2 ; Shipeng Li1 ; Charles D. Schwieters3 ; Yawen Bai1 ; baiyaw@mail.nih.gov" class="auth_mail" title="E-mail the corresponding author
- 关键词：GH5 ; globular domain of chicken H5 ; GH1 ; globular domain of Drosophila linker histone H1 ; ITC ; isothermal titration calorimetry ; MTSL ; [S-(2 ; 2 ; 5 ; 5-tetramethyl-2 ; 5-dihydro-1H-pyrrol-3-yl) methyl methanethiosulfonate] ; HMQC ; Heteronuclear Multiple-Quantum Correlation
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：9 October 2016
- 年：2016
- 卷：428
- 期：20
- 页码：3948-3959
- 全文大小：1699 K
文摘
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Methyl-transverse relaxation-optimized spectroscopy was used to study nucleosome binding by linker histones.
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Five residues in a linker histone can determine its location on the nucleosome.
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Different linker histone binding modes lead to distinct structures of chromatin.