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A NMR study of mobility in the histone octamer
Author(s) -
Schroth Gary P.,
Yau Peter,
Imai Brian S.,
Gatewood Joe M.,
Bradbury E.Morton
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80987-t
Subject(s) - histone octamer , trypsinization , histone , chemistry , nuclear magnetic resonance spectroscopy , chromatosome , crystallography , nucleosome , trypsin , biophysics , biochemistry , stereochemistry , biology , dna , enzyme
The histone octamer from chicken erythrocytes was studied in 2 M NaCI using 500 mHz 1 H 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.