Abstract
Among the more abundant non-histone proteins is the high mobility group (HMG), with an unknown role in chromatin. We have investigated, by chemical cross-linking, the interaction of the protein HMG 1 with the histone dimer H2A X H2B and the histone tetramer (H3 X H4)2 in free solution. Cross-linking with dimethyl suberimidate, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, and the cleavable cross-linker dimethyl-3,3'-dithiobispropionimidate, by two-dimensional electrophoresis reveals the existence of an interaction between HMG 1 and the histone dimer, and also between HMG 1 and the histone tetramer. In the case of the H2A X H2B dimer, the analysis of the patterns of the cross-linking products shows the presence of a trimer, (H2A X H2B) X HMG 1, and of another oligomer of higher molecular weight which also contains H2A X H2B and HMG 1. Non-histone HMG 1 has been found to interact with (H3 X H4)2, both by cross-linking kinetics and also by gel permeation chromatography, displaying a stoichiometry of one HMG 1/histone tetramer. The results have been interpreted as indicating the existence of an interaction between HMG 1 and both oligomers through two different binding sites.
Highlights
Among the moreabundant non-histone proteins is with the histone dimer H2A.H2B and the histone tetramer the high mobility group (HMG), with an unknown role (H3.H4)2 in free solutioAn.s far as we know, this is the first in chromatin
M, = 45,000and a broader one at apparent M, 60,000is IC, a differential disappearance of the monomeric H2B hinoticeable andis indicated by bovine serum albumin and stone can be seen, especially at long reaction time when the ovalbumin markers
These cross-linking bands were found cross-linking reaction occurs at pH 9.0, where the imidoesters
Summary
Among the moreabundant non-histone proteins is with the histone dimer H2A.H2B and the histone tetramer the high mobility group (HMG), with an unknown role (H3.H4)2 in free solutioAn.s far as we know, this is the first in chromatin. Cross-linking reactions were carried out at room have been interpreted as indicating the existenceof an interaction between HMG 1 and both oligomers through two different binding sites.
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