Open AccessSpin‐Label Study of Histone H1‐DNA Interaction
Author(s) -
GURARDET JeanLuc,
LAWRENCE JeanJacques
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07347.x
Subject(s) - chromatin , histone h1 , histone , dna , nucleosome , biophysics , histone code , chemistry , biology , genetics
As shown in a previous paper [J. J. Lawrence et al. (1980) Eur. J. Biochem. 107 , 263–269], convalent spin labeling of basis residues in histone H1 allows the study of the interaction of this protein with DNA. Using a step gradient dialysis procedure to reconstitute chromatin from labeled H1 and stripped chromatin, it is shown that the process of interaction of the lysine residures and DNA is the same whether histone H1 is bound to linear purified DNA or to H1‐depleted chromatin. In contrast, spin labeling of the unique tyrosine of histone H1 located in the globular part of the molecule shows that this part is more involved in the interaction with chromatin than it is with linear DNA (as judged from the lengthening of the rotational correlation time). These data are interpreted as reflecting defferent roles for th N and C termini of the molecule of H1 and the central globular part. A model, based on these observations together with examination of the primary structures of histones H1, is proposed which accounts for the H1 involvement in the chromatosome structure.