A NMR study of mobility in the histone octamer

FEBS Letters

Bradbury, E.Morton²  Gatewood, Joe M.¹  Imai, Brian S.¹  Schroth, Gary P.²  Yau, Peter² 

[1] Life Sciences Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA;Department of Biological Chemistry, School of Medicine, University of California, Davis, CA 95616, USA

关键词: Nuclear magnetic resonance;    Histone octamer;    Chromatin;    Trypsin;   

DOI  :  10.1016/0014-5793(90)80987-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The histone octamer from chicken erythrocytes was studied in 2 M NaCI using 500 mHz ¹H NMR spectroscopy. We compared the spectrum of control octamers with that of octamers isolated from trypsinized nucleosome core particles. We observe that the sharp resonances found in the spectrum of the native octamer disappear completely after trypsinization. Therefore, within the time frame of the NMR experiment, all of the mobile amino acid residues in the histone octamer are found in the well defined trypsin sensitive domains. These results indicate that there is a very clear structural demarcation between the random coil N- and C-terminal tails and the globular domains of the histones.

【 授权许可】

Unknown