Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. The conformation of phi1 histones from marine invertebrate sperm.
Proton magnetic resonance, circular dichroism and infrared spectroscopy are used to investigate the secondary and tertiary structure of three very lysine-rich histones from marine invertebrate sperm. At high ionic strength both Arbacia lixula and Holothuria tubulosa histone phi 1 are observed to contain 25-30% alpha-helix, no beta-structure and to form specific folded structures. Both phi 1 proton magnetic resonance spectra have perturbed methyl resonances at chemical shifts close to those observed for calf thymus H1, suggesting analogies in tertiary structure. Mytilus edulis histone phi 1 however, shows no spectroscopic evidence of secondary and tertiary structure on salt addition.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001974:Bromosuccinimide; D002843:Chromatin / Q000032:analysis* / Q000648:ultrastructure; D002942:Circular Dichroism; D004447:Echinodermata / Q000032:analysis*; D006657:Histones; D008239:Lysine / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D008974:Mollusca / Q000032:analysis*; D011487:Protein Conformation; D012617:Sea Urchins / Q000032:analysis*; D012623:Seawater; D013045:Species Specificity; D013094:Spermatozoa / Q000032:analysis*
D000596:Amino Acids; D002843:Chromatin; D006657:Histones; D008239:Lysine; D001974:Bromosuccinimide