This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Melton, T. Articles by Davis, A. T. Search for Related Content PubMed PubMed Citation Articles by Melton, T. Articles by Davis, A. T.

 Previous Article  |  Next Article 

J Bacteriol. 1978 February; 133(2): 708-716
Copyright © 1978 American Society for Microbiology. All Rights Reserved.

Chemotaxis of Salmonella typhimurium to Amino Acids and Some Sugars

Thoyd Melton, Philip E. Hartman, John P. Stratis, Timothy L. Lee and Alan T. Davis

¹ Department of Biology, The Johns Hopkins University, Baltimore, Maryland 21218

ABSTRACT

Patterns of chemotaxis by Salmonella typhimurium strain LT-2 to L-amino acids and to several sugars were quantitated by the Adler capillary procedure. Competition experiments indicated that LT-2 possesses three predominant receptors, or interacting sets of receptors, for amino acids. These were termed the aspartate, serine, and alanine classes, respectively. Studies with strains carrying point and deletion mutations affecting components of the phosphoenolpyruvate: glycose phosphotransferase system (PTS) made unlikely a role in primary reception of D-glucose by the three soluble PTS components, namely HPr, enzyme I, and factor III. A ptsG mutant defective in membrane-bound enzyme IIB' of the high-affinity glucose transport system was shown to exhibit normal chemotaxis providing pleiotropic effects of the mutation were eliminated by its genotypic combination with other pts mutations or, phenotypically, by addition of cyclic AMP and substrate. A correlation was demonstrated between chemotaxis to glucose and activity of the low-affinity glucose transport complex, membrane-bound enzymes IIB:IIA, and an enzyme IIB:IIA mutant was shown to have a preponderant defect in chemotaxis to glucose and mannose. Of four systems capable of galactose transport, only the ß-methylgalactoside transport system was implicated in chemotaxis to galactose. Some properties of a mutant possibly defective in processing of signals for chemotaxis to sugars is described.

Present address: Department of Microbiology, North Carolina State University at Raleigh, Raleigh, NC 27607

Present address: Fairleigh Dickinson University, Teaneck, NJ 07666.

Present address: Bard Hall, Columbia University College of Physicians and Surgeons, New York, NY 10032.

Present address: Department of Poultry Science, Cornell University, Ithaca, NY 14853.

Contribution no. 929 of the Department of Biology, Johns Hopkins University.