title: Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4.
abstract: The structural characterisation of protein-protein interactions is often challenging. Where interactions are not amenable to high-resolution approaches, alternatives providing lower resolution information are often of value. One such approach is site-directed cross-linking. Here, through the introduction of cysteine residues at strategic locations in histone proteins, we use site-directed cross-linking to monitor the association of chromatin subunits. This approach is informative for the study of both recombinant and native chromatin complexes consisting either of histone subunits alone or in association with accessory proteins, in this case histone chaperones. The approaches described may be generally applicable for monitoring the interactions of a diverse range of multi-protein complexes.
authors.affiliation: The Wellcome Trust Biocentre, University of Dundee, Dundee, Scotland, UK.
authors.forename: Andrew
authors.initials: A
authors.lastname: Bowman
authors.forename: Tom
authors.initials: T
authors.lastname: Owen-Hughes
mesh_terms: D000818:Animals; D020134:Catalytic Domain; D003432:Cross-Linking Reagents / Q000378:metabolism*; D006657:Histones / Q000737:chemistry*; D008967:Molecular Biology / Q000379:methods*; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D014982:Xenopus laevis
chemical_list: D003432:Cross-Linking Reagents; D006657:Histones; D013438:Sulfhydryl Compounds