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J Bacteriol. 1972 October; 112(1): 315-326
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Chemotaxis Toward Amino Acids in Escherichia coli

Robert Mesibov1 and Julius Adler2

Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706
Department of Genetics, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706

ABSTRACT

Escherichia coli cells are shown to be attracted to the L-amino acids alanine, asparagine, aspartate, cysteine, glutamate, glycine, methionine, serine, and threonine, but not to arginine, cystine, glutamine, histidine, isoleucine, leucine, lysine, phenylalanine, tryptophan, tyrosine, or valine. Bacteria grown in a proline-containing medium were, in addition, attracted to proline. Chemotaxis toward amino acids is shown to be mediated by at least two detection systems, the aspartate and serine chemoreceptors. The aspartate chemoreceptor was nonfunctional in the aspartate taxis mutant, which showed virtually no chemotaxis toward aspartate, glutamate, or methionine, and reduced taxis toward alanine, asparagine, cysteine, glycine, and serine. The serine chemoreceptor was nonfunctional in the serine taxis mutant, which was defective in taxis toward alanine, asparagine, cysteine, glycine, and serine, and which showed no chemotaxis toward threonine. Additional data concerning the specificities of the amino acid chemoreceptors with regard to amino acid analogues are also presented. Finally, two essentially nonoxidizable amino acid analogues, {alpha}-aminoisobutyrate and {alpha}-methylaspartate, are shown to be attractants for E. coli, demonstrating that extensive metabolism of attractants is not required for amino acid taxis.

J Bacteriol. 1972 October; 112(1): 315-326
Copyright © 1972 American Society for Microbiology. All Rights Reserved.



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