title: Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The isolation of the globular and non-globular regions of the histone H1 molecule.
abstract: Digestion of calf thymus H1 histone with thrombin cleaves the molecule at the sequence -(Pro)-Lys-Lys-Ala-, corresponding to a point approximately 122 residues from the N-terminus (about 56% along the molecule). The N-terminal fragment is shown by proton nuclear magnetic resonance (NMR) to possess the globular structure of the intact histome H1 molecule, whereas the C-terminal fragment appears to possess little or no structure. The N-terminal fragment separates into two peaks on an ion-exchange column, one of which is shown to originate from a single subfraction of calf thymus histone H1 and the other to originate from the other subfractions, by detailed comparison of the NMR spectra. It thus seems that the structure of the H1 histone in solution under physiological conditions consists of a globular head with a highly basic random coil tail. It is suggested that the globular head has a specific binding site on the subunit structure of the chromosome.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D005916:Globulins / Q000032:analysis*; D006657:Histones / Q000032:analysis*; D007700:Kinetics; D008239:Lysine / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy; D010447:Peptide Hydrolases; D011487:Protein Conformation; D013917:Thrombin; D013950:Thymus Gland
chemical_list: D000596:Amino Acids; D005916:Globulins; D006657:Histones; D010447:Peptide Hydrolases; D013917:Thrombin; D008239:Lysine