Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Nuclear-magnetic-resonance studies on nucleoprotein and histone phi 1-DNA complexes from marine invertebrate sperm.
Proton magnetic resonance and other measurements have been carried out in order to study the behaviour of the lysine-rich histones phi 1 in the sperm chromatin of certain marine invertebrates. Well defined particles (12 S) have been obtained from this chromatin by nuclease treatment. Chromatin solubility as a function of ionic strength shows a relaxation at salt concentrations higher than in the case of calf thymus nucleoprotein. Nuclear magnetic resonance (NMR) studies show that the release of histone from DNA occurs both in chromatin and in the reconstituted complexes at practically the same ionic strength as solubility relaxation. The higher the arginine content of a given phi 1, the higher the ionic strength at which both effects take place. The NMR results demonstrate that arginine residues are bound more strongly than lysine residues. The data overall show that phi 1 histones play a role in the contraction mechanism of sperm chromatin similar to that of H 1 histone in calf thymus chromatin. The highly contracted state of sperm chromatin is directly related to the increased arginine content of the phi 1 histone.
D000818:Animals; D001120:Arginine / Q000032:analysis; D002843:Chromatin / Q000378:metabolism*; D004247:DNA; D004447:Echinodermata; D006657:Histones / Q000502:physiology; D066298:In Vitro Techniques; D008239:Lysine / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D009698:Nucleoproteins; D011485:Protein Binding; D012617:Sea Urchins; D013094:Spermatozoa
D002843:Chromatin; D006657:Histones; D009698:Nucleoproteins; D004247:DNA; D001120:Arginine; D008239:Lysine