Intrasubunit nucleotide binding in ribonucleic acid polymerase.

Enzymatic Synthesis of Ribonucleic Acid. Iv. the Deoxyribonucleic Acid-directed Synthesis of Complementary Cytoplasmic Ribonucleic Acid Components.

The ribonucleic acid product formed by ribonucleic acid polymerase resembles its deoxyribonucleic acid template in base composition and in base sequence (l-6). The reaction in vitro results in the synthesis of RNA chains which are complementary to both DNA strands (6). Evidence for this originates from the formation of highly ordered RNA structures when the RNA polymerase product is annealed wi...

Appearance of a ribonucleic acid polymerase-binding protein in asporogenous mutants of Bacillus subtilis.

A 70,000-dalton protein that is found in sporulating Bacillus subtilis and that binds to ribonucleic acid polymerase is present in asporogenous mutants that proceed to or beyond stage II of sporulation, but is absent from mutants blocked at stage zero.

Binding sites on Escherichia coli ribonucleic acid polymerase.

Proflavine binding to transfer ribonucleic acid, synthetic ribonucleic acids, and deoxyribonucleic acid.

The ability of proflavine to directly inhibit protein synthesis has led to an investigation of complex formation between the drug and ribonucleic acid. Evidence has been obtained from absorption and fluorescence spectra, as well as heat denaturation curves, that proflavine forms a complex with transfer ribonucleic acid which is qualitatively similar to the deoxyribonucleic acid-proflavine compl...

Proflavine Binding to Transfer Ribonucleic Acid, Synthetic Ribonucleic Acids, and Deoxyribonucleic Acid*

The ability of proflavine to directly inhibit protein synthesis has led to an investigation of complex formation between the drug and ribonucleic acid. Evidence has been obtained from absorption and fluorescence spectra, as well as heat denaturation curves, that proflavine forms a complex with transfer ribonucleic acid which is qualitatively similar to the deoxyribonucleic acid-proflavine compl...