title: [RNA polymerase-rifamycin. A molecular model of inhibition].
abstract: By fluorimetric titration of Rifs (E. coli B) and Rifr (E. coli rpoB255) RNA polymerases with rifamycin, the mutant polymerase was demonstrated to bind rifamycin. A comparison of spatial structures of rifamycin and dinucleotide fragment of RNA in the hybrid with DNA revealed their similarity. Taking into account this structural similarity and also the fact that two phosphodiester bonds can be formed by RNA polymerase in the presence of rifamycin, a model for the inhibition mode was proposed. According to this model, rifamycin occupies the place of two terminal nucleotides of synthesized, but not translocated pentanucleotide in the transcribing complex. Asp-516 of the wild type beta-subunit was assumed to form a hydrogen bond with the rifamycin C(23) hydroxyl group. On the base of this model, reduced "cycling" synthesis of tetra-, penta-... up to decanucleotides by the Rifr RNA polymerase, in comparison with Rifs, was predicted.
mesh_terms: D012321:DNA-Directed RNA Polymerases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004352:Drug Resistance, Microbial; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D006860:Hydrogen Bonding; D008958:Models, Molecular; D012329:RNA, Bacterial / Q000096:biosynthesis*; D012294:Rifamycins / Q000378:metabolism / Q000494:pharmacology*
chemical_list: D012329:RNA, Bacterial; D012294:Rifamycins; C033974:rifamycin B; D012321:DNA-Directed RNA Polymerases
vernacular_title: RNK-polimeraza-rifamitsin. Molekuliarnaia model' ingibirovaniia.