RNA polymerase: interaction of RNA and rifampicin with the subassembly alpha 2 beta.
We studied the inhibition of tryptic digestion of the subassembly alpha 2 beta of Escherichia coli DNA-dependent RNA polymerase to investigate its interaction with RNA and rifampicin. Both agents decreased distinctly the cleavage of subunit beta in the subassembly as well as the degradation of the transiently formed polypeptides (Mr greater than 80000). Short RNAs with a chain length of approximately 35 nucleotides were most protective at a concentration of 1 mg/ml while long RNAs were less effective at the same concentration. DNA did not exert any observable protective effects. The association of RNA with alpha 2 beta was shown by chromatography on phosphocellulose, which separates alpha 2 beta bound to RNA from free alpha 2 beta. The association of alpha 2 beta with RNA was inhibited by rifampicin.
D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D046911:Macromolecular Substances; D009690:Nucleic Acid Conformation; D012313:RNA / Q000378:metabolism*; D012293:Rifampin / Q000378:metabolism*; D012441:Saccharomyces cerevisiae; D014357:Trypsin / Q000378:metabolism
D046911:Macromolecular Substances; D012313:RNA; D012321:DNA-Directed RNA Polymerases; D014357:Trypsin; D012293:Rifampin