Accessibility of an epitope common to all histone H3 variants in folded and unfolded chromatin as studied by a monoclonal antibody.
In a recent publication the isolation and some characteristics of an anti-histone 3 monoclonal antibody, 1GB3 were described (Muller et al. FEBS Lett. 182: 459-464, 1985). We now report that the epitope recognized is phylogenetically conserved and located in the N-terminal part of H3, most likely between residues 40 and 50. Using the ELISA technique we found this region to be accessible in chromatin to the monoclonal antibody. The effect of non-ionic detergents on the adsorbtion of chromatin on microtiter plates was studied in this context. Immunological analysis of the reaction of the monoclonal antibody with chromatin by immunoinhibition and immunosedimentation shows that the H3 epitope is accessible in both folded and unfolded chromatin fibre as well as in high- and low-molecular weight oligonucleosomes.
Jockers-Wretou
E
E
Institut Pasteur Hellenique, Athens, Greece.
Russanova
V
V
Venkov
C
C
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D002843:Chromatin / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology*; D005455:Fluorescent Antibody Technique; D006657:Histones / Q000276:immunology*; D015151:Immunoblotting; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D002843:Chromatin; D000939:Epitopes; D006657:Histones