Showing papers by "Paul Doty published in 1975"

Chemical and physical properties of fractionated chromatin.

Abstract: Sonicated chicken reticulocyte chromatin was fractionated into transcriptionally active and transcriptionally repressed components. The active fraction is 8% of the whole chromatin but contains 70% of the newly synthesized chromosomal RNA. This RNA has five times as many hemoglobin RNA sequences as does the RNA in the repressed fraction. The amount of the active fraction in the chromatins of several tissues correlates with their synthetic activity. The molecular weight of the DNA of the repressed fraction is approximately twice that of the active fraction. Moreover, the configuration of repressed chromatin is much more compact, consistent with a much larger sedimentation constant. The transcriptionally active fraction displays a 6 degrees lower melting profile and is highly susceptible to DNase I relative to the repressed fraction. The active fraction contains twice as much non-histone protein and 15% less histone than the repressed fraction and is lacking the lysine-rich and much of the arginine-rich histones.

A comparison of the binding to polynucleotides of complementary and noncomplementary oligonucleotides.

Abstract: The binding of oligonucleotides to synthetic polynucleotides has been studied as a control for investigations of the binding of oligonucleotides to natural RNA molecules. Only combinations that involved A-U, G-C, and G-G pairs were found to be significantly stable under the experimental conditions used here. The stability of the oligomerpolymer pairing increased with the length of the region paired and with its G + C content. Further, some different sequence isomers of the same G + C content exhibited quite different binding constants. This variability is consistent with certain sequence differences in the double-strand stacking interactions stabilizing the oligomer-polymer association. Oligomer binding was also shown to depend upon the identity of the polymer residues neighboring the binding site, indicating the effect upon oligomer binding of small changes in the single-strand conformation of the binding site. These observations validate the criteria that allow one to decide if an observed association constant of an oligomer to an RNA molecule reflects a complete complementarity between the two or not. This improves the basis for using oligonucleotide binding constants to RNA of known sequences to map secondary structure.