Folding of 140-base pair length DNA by a core of arginine-rich histones.
The nucleoprotein complex obtained by reconstitution of arginine-rich histones with 140-base pair length DNA has properties considerably closer to native core particles than the complex obtained with lysine-rich histones. A tetramer of arginine-rich histones folds 140-base pair length DNA into a particle (R body) with identical projections, on high resolution electron micrographs, as native core particles. The R body is more spherical in shape than the native nucleosome core particle. Both arginine- and lysine-rich histones contribute to the altered thermal stability and circular dichroism spectra of the core particle DNA.
D000818:Animals; D001120:Arginine; D002645:Chickens; D002942:Circular Dichroism; D003852:Deoxyribonucleoproteins; D004912:Erythrocytes; D006657:Histones; D007700:Kinetics; D008854:Microscopy, Electron; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D009698:Nucleoproteins; D011487:Protein Conformation
D003852:Deoxyribonucleoproteins; D006657:Histones; D009698:Nucleoproteins; D001120:Arginine