This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yanofsky, C
Right arrow Articles by Gollnick, P
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yanofsky, C
Right arrow Articles by Gollnick, P

 Previous Article  |  Next Article 

J Bacteriol. 1991 October; 173(19): 6009-6017

research-article

Physiological studies of tryptophan transport and tryptophanase operon induction in Escherichia coli.

C Yanofsky, V Horn and P Gollnick

Department of Biological Sciences, Stanford University, California 94305-5020.

ABSTRACT

Escherichia coli forms three permeases that can transport the amino acid tryptophan: Mtr, AroP, and TnaB. The structural genes for these permeases reside in separate operons that are subject to different mechanisms of regulation. We have exploited the fact that the tryptophanase (tna) operon is induced by tryptophan to infer how tryptophan transport is influenced by the growth medium and by mutations that inactivate each of the permease proteins. In an acid-hydrolyzed casein medium, high levels of tryptophan are ordinarily required to obtain maximum tna operon induction. High levels are necessary because much of the added tryptophan is degraded by tryptophanase. An alternate inducer that is poorly cleaved by tryptophanase, 1-methyltryptophan, induces efficiently at low concentrations in both tna+ strains and tna mutants. In an acid-hydrolyzed casein medium, the TnaB permease is most critical for tryptophan uptake; i.e., only mutations in tnaB reduce tryptophanase induction. However, when 1-methyltryptophan replaces tryptophan as the inducer in this medium, mutations in both mtr and tnaB are required to prevent maximum induction. In this medium, AroP does not contribute to tryptophan uptake. However, in a medium lacking phenylalanine and tyrosine the AroP permease is active in tryptophan transport; under these conditions it is necessary to inactivate the three permeases to eliminate tna operon induction. The Mtr permease is principally responsible for transporting indole, the degradation product of tryptophan produced by tryptophanase action. The TnaB permease is essential for growth on tryptophan as the sole carbon source. When cells with high levels of tryptophanase are transferred to tryptophan-free growth medium, the expression of the tryptophan (trp) operon is elevated. This observation suggests that the tryptophanase present in these cells degrades some of the synthesized tryptophan, thereby creating a mild tryptophan deficiency. Our studies assign roles to the three permeases in tryptophan transport under different physiological conditions.

J Bacteriol. 1991 October; 173(19): 6009-6017




This article has been cited by other articles:

  • Kwon, Y.-M., Weiss, B. (2009). Production of 3-Nitrosoindole Derivatives by Escherichia coli during Anaerobic Growth. J. Bacteriol. 191: 5369-5376 [Abstract] [Full Text]  
  • Zhang, Y., Hong, G. (2009). Evidences of Hfq associates with tryptophanase and affects extracellular indole levels. Acta Biochim Biophys Sin 41: 709-717 [Abstract] [Full Text]  
  • Yang, R., Cruz-Vera, L. R., Yanofsky, C. (2009). 23S rRNA Nucleotides in the Peptidyl Transferase Center Are Essential for Tryptophanase Operon Induction. J. Bacteriol. 191: 3445-3450 [Abstract] [Full Text]  
  • Mueller, R. S., Beyhan, S., Saini, S. G., Yildiz, F. H., Bartlett, D. H. (2009). Indole Acts as an Extracellular Cue Regulating Gene Expression in Vibrio cholerae. J. Bacteriol. 191: 3504-3516 [Abstract] [Full Text]  
  • Lee, J., Maeda, T., Hong, S. H., Wood, T. K. (2009). Reconfiguring the Quorum-Sensing Regulator SdiA of Escherichia coli To Control Biofilm Formation via Indole and N-Acylhomoserine Lactones. Appl. Environ. Microbiol. 75: 1703-1716 [Abstract] [Full Text]  
  • Nikaido, E., Yamaguchi, A., Nishino, K. (2008). AcrAB Multidrug Efflux Pump Regulation in Salmonella enterica serovar Typhimurium by RamA in Response to Environmental Signals. J. Biol. Chem. 283: 24245-24253 [Abstract] [Full Text]  
  • Stewart, V. (2008). The Ribosome: a Metabolite-Responsive Transcription Regulator. J. Bacteriol. 190: 4787-4790 [Full Text]  
  • Bernasconi, C., Volponi, G., Picozzi, C., Foschino, R. (2007). Use of the tna Operon as a New Molecular Target for Escherichia coli Detection. Appl. Environ. Microbiol. 73: 6321-6325 [Abstract] [Full Text]  
  • Lee, J., Bansal, T., Jayaraman, A., Bentley, W. E., Wood, T. K. (2007). Enterohemorrhagic Escherichia coli Biofilms Are Inhibited by 7-Hydroxyindole and Stimulated by Isatin. Appl. Environ. Microbiol. 73: 4100-4109 [Abstract] [Full Text]  
  • Gong, M., Cruz-Vera, L. R., Yanofsky, C. (2007). Ribosome Recycling Factor and Release Factor 3 Action Promotes TnaC-Peptidyl-tRNA Dropoff and Relieves Ribosome Stalling during Tryptophan Induction of tna Operon Expression in Escherichia coli. J. Bacteriol. 189: 3147-3155 [Abstract] [Full Text]  
  • Quick, M., Yano, H., Goldberg, N. R., Duan, L., Beuming, T., Shi, L., Weinstein, H., Javitch, J. A. (2006). State-dependent Conformations of the Translocation Pathway in the Tyrosine Transporter Tyt1, a Novel Neurotransmitter:Sodium Symporter from Fusobacterium nucleatum. J. Biol. Chem. 281: 26444-26454 [Abstract] [Full Text]  
  • Domka, J., Lee, J., Wood, T. K. (2006). YliH (BssR) and YceP (BssS) Regulate Escherichia coli K-12 Biofilm Formation by Influencing Cell Signaling. Appl. Environ. Microbiol. 72: 2449-2459 [Abstract] [Full Text]  
  • Rezwan, F., Lan, R., Reeves, P. R. (2004). Molecular Basis of the Indole-Negative Reaction in Shigella Strains: Extensive Damages to the tna Operon by Insertion Sequences. J. Bacteriol. 186: 7460-7465 [Abstract] [Full Text]  
  • Androutsellis-Theotokis, A., Goldberg, N. R., Ueda, K., Beppu, T., Beckman, M. L., Das, S., Javitch, J. A., Rudnick, G. (2003). Characterization of a Functional Bacterial Homologue of Sodium-dependent Neurotransmitter Transporters. J. Biol. Chem. 278: 12703-12709 [Abstract] [Full Text]  
  • Yanofsky, C. (2003). Using Studies on Tryptophan Metabolism to Answer Basic Biological Questions. J. Biol. Chem. 278: 10859-10878 [Full Text]  
  • Diaz, E., Ferrandez, A., Prieto, M. A., Garcia, J. L. (2001). Biodegradation of Aromatic Compounds by Escherichia coli. Microbiol. Mol. Biol. Rev. 65: 523-569 [Abstract] [Full Text]  
  • Wang, D., Ding, X., Rather, P. N. (2001). Indole Can Act as an Extracellular Signal in Escherichia coli. J. Bacteriol. 183: 4210-4216 [Abstract] [Full Text]  
  • Santillan, M., Mackey, M. C. (2001). Dynamic regulation of the tryptophan operon: A modeling study and comparison with experimental data. Proc. Natl. Acad. Sci. USA 98: 1364-1369 [Abstract] [Full Text]  
  • Baumann, C., Otridge, J., Gollnick, P. (1996). Kinetic and Thermodynamic Analysis of the Interaction between TRAP (trp RNA-binding Attenuation Protein) of Bacillus subtilis and trp Leader RNA. J. Biol. Chem. 271: 12269-12274 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»