Interaction of bovine seminalplasmin with Escherichia coli RNA polymerase in the presence of rifampicin.
The interaction of bovine seminalplasmin and rifampicin with E. coli RNA polymerase was studied using fluorescence spectroscopy. Both seminalplasmin and rifampicin are known to be the inhibitors for the initiation of RNA synthesis in E. coli. Rifampicin quenced the intrinsic fluorescence of RNA polymerase and seminalplasmin when excited at 280 nm. However, excess of seminalplasmin reversed the quenching of RNA polymerase fluorescence by rifampicin. Upon addition of rifampicin to the seminalplasmin-RNA polymerase complex, no change in fluorescence spectrum was observed. It appeared that although rifampicin could form complexes with RNA polymerase and seminalplasmin alone, no binding domain was available for rifampicin in the RNA polymerase-seminalplasmin complex. These observations are discussed in the light of the 'initiation site' of E. coli RNA polymerase.
D000818:Animals; D002417:Cattle; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D011506:Proteins / Q000378:metabolism*; D012293:Rifampin / Q000494:pharmacology*; D029607:Seminal Vesicle Secretory Proteins; D013050:Spectrometry, Fluorescence
D011506:Proteins; D029607:Seminal Vesicle Secretory Proteins; D012321:DNA-Directed RNA Polymerases; D012293:Rifampin