Photo-induced crosslinking of histones H3 and H1 to DNA in deoxyribonucleoprotein: implication in studying histone-DNA interactions.
A thymine-modified derivative of histone H3, isolated as a result of heat treatment of covalently crosslinked DNA-protein photoadduct from UV-irradiated chromatin, was obtained. Sequence analysis of one of its tryptic peptides revealed that lysine-14 of the N-terminal tail of the histone H3 molecule covalently binds to thymine residue of DNA. This type of UV-crosslinking is most probably the only type for histone H3 and, possibly, for H1.
Kurochkina
L
L
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, USSR.
Kolomijtseva
G
G
D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003432:Cross-Linking Reagents; D004247:DNA / Q000378:metabolism*; D003852:Deoxyribonucleoproteins / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006358:Hot Temperature; D008239:Lysine / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D010449:Peptide Mapping; D010777:Photochemistry; D014357:Trypsin; D014466:Ultraviolet Rays
D003432:Cross-Linking Reagents; D003852:Deoxyribonucleoproteins; D006657:Histones; D010446:Peptide Fragments; D004247:DNA; D014357:Trypsin; D008239:Lysine