Close contacts between H1 histone molecules in nuclei.
H1 histone homodimer has been purified from nuclei treated with either long (dimethylsuberimidate, dimethyl dithiobisproprionimidate) or short (ethyl dimethylaminocarbodiimide) cross-linking reagents. When such H1 dimers were cleaved with N-bromosuccinimide, chymotrypsin, or staphylococcal protease, analysis of the resulting fragments suggests that the major cross-links were formed between the COOH-terminal portions of neighboring H1 molecules, and that substantial bridging can also be made between the NH2-terminal portion of one H1 molecule and the COOH-terminal portion of another. NH2-terminal to NH2-terminal cross-links were not seen at significant levels, suggesting that the position of the NH2-terminal portion of H1 in chromatin is more restricted.
D000595:Amino Acid Sequence; D000818:Animals; D001974:Bromosuccinimide / Q000494:pharmacology; D002417:Cattle; D002467:Cell Nucleus / Q000032:analysis*; D002918:Chymotrypsin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D006657:Histones / Q000032:analysis*; D007668:Kidney / Q000648:ultrastructure; D008297:Male; D008666:Metalloendopeptidases; D008970:Molecular Weight
D006657:Histones; D010450:Endopeptidases; D002918:Chymotrypsin; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus; D001974:Bromosuccinimide