title: Circular dichroism studies on chromatin models. Interactions between DNA and sequential polypeptides containing arginine.
abstract: The sequential polypeptides (L-Arg-Xaa-Gly)n where Xaa represents amino acid residues Ala, Val and Leu, were employed as models of arginine-rich histones, in studying their interactions with nucleic acids. These polypeptide-DNA complexes were prepared using gradient dialysis and their conformational properties were investigated by circular dichroism spectroscopy. It was found that poly(L-Arg-L-Val-Gly) caused pronounced structural changes in the DNA molecule (conformational transition from B to the more compact and asymmetric C form) as a function of ionic strength and polypeptide: DNA ratio. In contrast the DNA interaction with poly (L-Arg-L-Ala-Gly) and poly (L-Arg-L-Leu-Gly) increased in the order of Ala----Leu, but with slight structural changes in the DNA secondary conformation. Thus, the importance of the composition, amino acid sequence and conformation of the polypeptides which bind to DNA was demonstrated. The significance of the hydrophobic forces besides the arginine-phosphate charge interaction, which modulate the nature of the polypeptide-DNA complexes and their condensation into higher-ordered tertiary structures, as found in chromatin, was also confirmed.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000032:analysis; D001483:Base Sequence; D002417:Cattle; D002843:Chromatin / Q000378:metabolism*; D002942:Circular Dichroism; D004247:DNA / Q000378:metabolism*; D006657:Histones / Q000032:analysis; D046911:Macromolecular Substances / Q000378:metabolism*; D008956:Models, Chemical; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship
chemical_list: D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D004247:DNA; D001120:Arginine