ABSTRACT
Template chromatography using immobilized nucleotides or peptides provides a very powerful tool for studying the mechanism of peptide-nucleotide interactions. The peptide-oligonucleotide interaction decreases considerably when nonaromatic amino acids are present in the peptide. Naturally occurring peptides and proteins that contain relatively small amounts of tryptophan. Selectivity of the lysine peptide-oligonucleotide interaction occurs only if the positively charged groups are arranged in a specific mode. The mechanism of action of transfer ribonucleic acid (tRNA) methylases has been investigated using aminohydroxybutyl cellulose which was linked with each of the individual tRNAs through their oxidized 3’ termini. The reaction products with the use of five purified histone classes were all found to be bound more tightly to DNA-cellulose than to the enzyme-bound polymer. The use of an early reaction product of tritium-labeled oligo(adenosine-5'-diphosphate (ADP)-ribosyl) enzyme clearly indicated that no ADP-ribose covalently bound to the enzyme is transferred to histone.
