DNA-protein interactions in nucleosomes and in chromatin. Structural studies of chromatin stabilized by ultraviolet-light induced crosslinking.
Crosslinking induced by ultraviolet light irradiation at 254 nm has been utilized to investigate the structure of chromatin and isolated nucleosomes. The results presented here imply that the four core histones, as well as histone H1, have reactive groups within a bond length of the DNA bases. In nucleosomes depleted of H1, all of the core histones react similarly with the DNA and form crosslinks. In chromatin, the rate of crosslinking of all histones to DNA is essentially similar. Comparison of mononucleosomes, dinucleosomes and whole chromatin shows that the rate of crosslinking increases significantly with increasing number of connected nucleosomes. These differences in the rate of crosslinking are interpreted in terms of interactions between neighbouring nucleosomes on the chromatin fiber, which are absent in an isolated mononucleosome.
D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000528:radiation effects* / Q000648:ultrastructure; D002843:Chromatin / Q000528:radiation effects* / Q000648:ultrastructure; D004247:DNA / Q000528:radiation effects; D003852:Deoxyribonucleoproteins / Q000528:radiation effects; D006657:Histones; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009698:Nucleoproteins / Q000528:radiation effects; D013950:Thymus Gland; D014466:Ultraviolet Rays
D002843:Chromatin; D003852:Deoxyribonucleoproteins; D006657:Histones; D046911:Macromolecular Substances; D009698:Nucleoproteins; D004247:DNA