Identification of interacting amino acids at the histone 2A-2B binding site
- 1 May 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (10), 1942-1946
- https://doi.org/10.1021/bi00577a014
Abstract
Histones 2A and 2B of calf thymus were cross-linked within intact nuclei by UV-irradiation. This procedure induces the formation of covalent cross-links between noncovalently interacting residues in the histones of native chromatin. Tryptic peptide and partial sequence analysis of the cross-linked product showed that the covalent linkage is between tyrosine-37, -40 or -42 of H2B and proline-26 of H2A. These residues constitute part of the hydrophobic H2A-H2B binding domain within the nucleosomes of native chromatin.This publication has 7 references indexed in Scilit:
- Amino acid contacts between histones are the same for plants and mammals. Binding-site studies with ultraviolet and tetranitromethane crosslinkingBiochemistry, 1979
- Histone-histone interactions within chromatin. Preliminary location of multiple contact sites between histones 2A, 2B and 4Biochemistry, 1979
- ChromatinNature, 1978
- DNA-binding Segments of Four Histone Sequences Identified in Trypsin-treated H1-depleted Chromatin1The Journal of Biochemistry, 1977
- PEA HISTONES-H2A AND HISTONES-H2B - VARIABLE AND CONSERVED REGIONS IN SEQUENCES1977
- Histone-histone interactions within chromatin. Preliminary characterization of presumptive H2B-H2A and H2B-H4 binding sitesBiochemistry, 1976
- Histone-histone interactions within chromatin. Crosslinking studies using ultraviolet lightBiochemistry, 1976