Biomedical subjects
Publications and source records attributed to J Adler.
Motile bacteria presented simultaneously with both attractant and repellent respond to whichever one is present in the more effective concentration. Apparently bacteria have a processing mechanism that compares opposing signals from the chemoreceptors for positive and negative taxis, sums these signals up, and then communicates the sum to the flagella.
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The source of energy for bacterial motility is the intermediate in oxidative phosphorylation, not ATP directly. For chemotaxis, however, there is an additional requirement, presumably ATP. These conclusions are based on the following findings. (i) Unlike their parents, mutants of Escherichia coli and Salmonella typhimurium that are blocked in the conversion of ATP to the intermediate of oxidative phosphorylation failed to swim anaerobically, even when they produced ATP. When respiration was restored to the mutants, motility was simultaneously restored. (ii) Carbonylcyanide m-chlorophenylhydrazone, which uncouples oxidative phosphorylation, completely inhibited motility even though ATP remained present. (iii) Arsenate did not inhibit motility in the presence of an oxidizable substrate, though it did reduce ATP levels to less than 0.3% (iv) Arsenate completely inhibited chemotaxis under conditions where motility was normal.
For D-glucose and analogs there are two distinct phosphotransferase enzymes II with different specificities. Transport and chemotaxis were studied in E. coli mutants having only one or the other of these two enzymes. It was found that the transport specificity of a given enzyme II correlates with taxis specificity, and mutational loss of an enzyme II abolishes taxis toward only those sugars which it alone transports. Although enzyme I and the phosphate-carrier protein are required for full D-glucose taxis, it could not be determined if phosphorylation and transport are also required.
By using a new screening method, we have obtained 43 new Escherichia coli mutants defective in ring formation on galactose swarm plates, which score for defects in chemotaxis or transport. They were complemented and compared with mutations previously known to lie in the galactose-binding protein or the beta-methylgalactoside (mgl) permease, or both. The mutations were all found to lie in three genes, called mglA, mglB, and mglC. mglB codes for the gene specifying the binding protein. Based on co-transduction experiments, mglA, mglB, and mglC lie close to each other on the bacterial chromosome.
beta-Methylgalactoside (mgl) permease mutants of Escherichia coli, which are defective in three genes, mglA, mglB, and mglC, were assayed for galactose taxis and galactose transport. The mglB product is the galactose-binding protein. Previous evidence, supported by our new findings, shows that the galactose-binding protein is the recognition component for galactose taxis as well as for galactose transport. Most mutants defective in mglB showed strong effects on both chemotaxis and transport; however, a couple showed effects chiefly on one process or the other, thus allowing a separation of chemotaxis and transport. The mglA and mglC products have not yet been identified, but they must be components of the galactose transport machinery since mutants defective in mglA or mglC, or both, showed strongly reduced transport. Although some of these mutants showed little chemotaxis, most gave close to wild-type chemotactic responses. Thus, transport is not required for galactose taxis. The bacteria detect changes in the fraction of binding protein associated with galactose, not changes in the rate of transport.
Several methods for detecting or measuring negative chemotaxis are described. Using these, we have surveyed a number of chemicals for their ability to repel Escherichia coli. Although most of the repellents are harmful compounds, harmfulness is neither necessary nor sufficient to make a compound a repellent. The repellents can be grouped into at least nine classes according to (i) competition experiments, (ii) mutants lacking certain of the negative taxes, and (iii) their chemical structure. The specificity of each class was studied. It is suggested that each class corresponds to a distinct chemoreceptor. Generally, non-chemotactic mutants lack both positive and negative chemotaxis, and l-methionine is required for both kinds of taxis. Repellents at very low concentrations are not attractants, and attractants at very high concentrations are not repellents.
Virus-like particles were purified from a single nonaflatoxin-producing isolate of Aspergillus flavus. The virus-like particles were spherical, measuring 27 to 30 nm in diameter, were electrophoretically homogeneous, and sedimented at approximately 49S. The particles had a buoyant density of 1.28 g/cm(3) in CsCl and contained no detectable nucleic acid.
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Attractant was added to a suspension of bacteria (the background concentration of attractant) and then these bacteria were exposed to a yet higher concentration of attractant in a capillary. Chemotaxis was measured by determining how many bacteria accumulated in the capillary. The response range for chemotaxis lies between the threshold concentration and the saturating concentration. The breadth of this range is different for attractants detected by different chemoreceptors. Attractants detected by the same chemoreceptor can have their response ranges in widely different places. Over the center of the response range (on a logarithmic scale), bacteria give similar sized responses to similar fractional increases of concentration, i.e. they respond to ratios of attractant concentration, but the response peaks at the center of the range. The size of the response is different for attractants detected by different chemoreceptors. For a detectable response, a smaller increase in attractant concentration is needed for attractants detected by some chemoreceptors than for attractants detected by others. Although the data are inadequate, it appears that the Weber law may be observed over a wide range of concentrations for some attractants but not for others. In the Appendix we aim to explain some of these results in terms of the interaction of an attractant with its chemoreceptor according to the law of mass action.
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Using a quantitative assay for measuring chemotaxis, we tested a variety of sugars and sugar derivatives for their ability to attract Escherichia coli bacteria. The most effective attractants, i.e., those that have thresholds near 10(-5) M or below, are N-acetyl-d-glucosamine, 6-deoxy-d-glucose, d-fructose, d-fucose, 1-d-glycerol-beta-d-galactoside, galactitol, d-galactose, d-glucosamine, d-glucose, alpha-d-glucose-1-phosphate, lactose, maltose, d-mannitol, d-mannose, methyl-beta-d-galactoside, methyl-beta-d-glucoside, d-ribose, d-sorbitol, and trehalose. Lactose, and probably d-glucose-1-phosphate, are attractive only after conversion to the free monosaccharide, while the other attractants do not require breakdown for taxis. Nine different chemoreceptors are involved in detecting these various attractants. They are called the N-acetyl-glucosamine, fructose, galactose, glucose, maltose, mannitol, ribose, sorbitol, and trehalose chemoreceptors; the specificity of each was studied. The chemoreceptors, with the exception of the one for d-glucose, are inducible. The galactose-binding protein serves as the recognition component of the galactose chemoreceptor. E. coli also has osmotically shockable binding activities for maltose and d-ribose, and these appear to serve as the recognition components for the corresponding chemoreceptors.
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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.
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