Interaction of histone H1 from sea urchin sperm with superhelical and relaxed DNA.
Complexes of histone H1 from sea urchin sperm (H1S) and calf thymus (H1T) with superhelical DNA I and relaxed circular DNA II have been analyzed by analytical sedimentation. Similar to H1T, the highly basic and relatively arginine-rich histone H1S preferentially interacts with DNA I compared to DNA II under competition conditions. However, H1S induces a stronger aggregation of both forms of DNA than H1T. Below 0.05 M NaCl, the soluble complexes formed by both histones have similar properties, but aggregation proceeds in a different manner: H1S induces a stronger aggregation of DNA II as compared to DNA I, whereas H1T fails to aggregate DNA I. The results are explained on the basis of differences in amino acid sequence and structure of the two histones and related to the special chromatin condensing ability of histone H1S.
D000818:Animals; D001667:Binding, Competitive; D004270:DNA, Circular / Q000378:metabolism*; D004278:DNA, Superhelical / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D066298:In Vitro Techniques; D008297:Male; D011487:Protein Conformation; D012617:Sea Urchins / Q000378:metabolism*; D012995:Solubility; D013094:Spermatozoa / Q000378:metabolism*; D013950:Thymus Gland / Q000378:metabolism
D004270:DNA, Circular; D004278:DNA, Superhelical; D006657:Histones