The effect of protein modification reagents on the chemotactic response in Salmonella typhimurium.
Several classes of reagents that covalently modify proteins have been shown to inhibit the ability of Salmonella typhimurium to reverse the direction of its flagellar rotation. Such reversal normally allows the bacterium to tumble and reorient its movement in a more favorable direction. These reagents include those that react with amino, guanidino, sulfhydryl, and disulfide groups on proteins. At high concentrations, most of these compounds also cause the paralysis of flagellar rotation. Tumbling in bacterial chemotaxis has been shown to be dependent on the methylation of a class of membrane proteins. The effects of these reagents in an in vitro methylation system have been studied. The results obtained suggest that most of these compounds are probably not acting on intact cells by inhibiting the activities of the cheR methyltransferase or the methyl-accepting proteins.
D000447:Aldehydes / Q000494:pharmacology; D002633:Chemotaxis / Q000187:drug effects*; D003512:Cyclohexanones / Q000494:pharmacology; D003931:Diacetyl / Q000494:pharmacology; D005407:Flagella / Q000502:physiology; D008745:Methylation; D012486:Salmonella typhimurium / Q000502:physiology*; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D013439:Sulfhydryl Reagents / Q000494:pharmacology*
D000447:Aldehydes; D003512:Cyclohexanones; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents; D003931:Diacetyl