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Relaxation of chromatin structure upon removal of histones H2A and H2B
Author(s) -
Jordano Juan,
Montero Francisco,
Palacián Enrique
Publication year - 1984
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(84)80876-5
Subject(s) - chromatin , histone , circular dichroism , chemistry , biophysics , histone modifying enzymes , histone h1 , dna , nucleosome , histone h2b , biochemistry , crystallography , biology
Modification of chromatin from chicken erythrocytes with dimethylmaleic anhydride is accompanied by its solubilization and the dissociation of histones H1, H5, H2A and H2B. Histone H1 is the first to dissociate and H5 the last. After regeneration of the modified amino groups, residual chromatin preparations with different histone composition were studied by circular dichroism and thermal denaturation. In addition to the effects produced by the lack of histones HI and H5, both techniques show a substantial relaxation of chromatin structure induced by the loss of histones H2A and H2B, which appear to play an important role in the superhelical folding of DNA.