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 HighWire Citing Articles via Google Scholar Google Scholar Articles by Koman, A. Articles by Hazelbauer, G. L. Search for Related Content PubMed PubMed Citation Articles by Koman, A. Articles by Hazelbauer, G. L.

 Previous Article  |  Next Article 

J Bacteriol. 1979 June; 138(3): 739-747
Copyright © 1979, American Society for Microbiology. All Rights Reserved.

Relation of Chemotactic Response to the Amount of Receptor: Evidence for Different Efficiencies of Signal Transduction

The Membrane Group, The Wallenberg Laboratory, University of Uppsala, S-752 37 Uppsala, Sweden

ABSTRACT

We determined the content of galactose-glucose-, maltose-, and ribose-binding proteins in cells of Escherichia coli K-12 grown in a variety of media and also measured the respective transport and chemotactic activities that depend on those binding proteins. Correlation of the level of induction of a particular binding protein with the extent of tactic activity mediated by that protein indicates that the magnitude of the tactic response to a particular stimulating compound is a direct function of the number of receptors per cell. In contrast, comparison of the magnitudes of response to substances recognized by independent receptors indicates that some stimulus-receptor complexes are more effective in eliciting tactic responses than are others. Thus, the magnitude of response to any particular stimulating compound is a function both of the number of receptors per cell and of the effectiveness of the stimulus-receptor complex. Considerations of available information about the tactic response to maltose suggest that the effectiveness of a stimulus-receptor complex is related to the transducer with which the receptor interacts. The tar product appears to be a relatively effective transducer of the signals it accepts from receptors for aspartate, -methylaspartate, and maltose, whereas the trg product appears to be a relatively ineffective transducer of signals it accepts from receptors for galactose and ribose.

This article has been cited by other articles:

• Post, D. M. B., Mungur, R., Gibson, B. W., Munson, R. S. Jr. (2005). Identification of a Novel Sialic Acid Transporter in Haemophilus ducreyi. Infect. Immun. 73: 6727-6735 [Abstract] [Full Text]  
• Sprencel, C., Cao, Z., Qi, Z., Scott, D. C., Montague, M. A., Ivanoff, N., Xu, J., Raymond, K. M., Newton, S. M. C., Klebba, P. E. (2000). Binding of Ferric Enterobactin by the Escherichia coli Periplasmic Protein FepB. J. Bacteriol. 182: 5359-5364 [Abstract] [Full Text]  
• Weerasuriya, S., Schneider, B. M., Manson, M. D. (1998). Chimeric Chemoreceptors in Escherichia coli: Signaling Properties of Tar-Tap and Tap-Tar Hybrids. J. Bacteriol. 180: 914-920 [Abstract] [Full Text]