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 Horlacher, R.
Right arrow Articles by Boos, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Horlacher, R.
Right arrow Articles by Boos, W.

 Previous Article  |  Next Article 

J. Bacteriol., Nov 1996, 6250-6257, Vol 178, No. 21
Copyright © 1996, American Society for Microbiology

Characterization of a cytoplasmic trehalase of Escherichia coli

R Horlacher, K Uhland, W Klein, M Ehrmann and W Boos
Department of Biology, University of Konstanz, Germany.

Escherichia coli can synthesize trehalose in response to osmotic stress and is able to utilize trehalose as a carbon source. The pathway of trehalose utilization is different at low and high osmolarity. At high osmolarity, a periplasmic trehalase (TreA) is induced that hydrolyzes trehalose in the periplasm to glucose. Glucose is then taken up by the phosphotransferase system. At low osmolarity, trehalose is taken up by a trehalose-specific enzyme II of the phosphotransferase system as trehalose-6-phosphate and then is hydrolyzed to glucose and glucose-6- phosphate. Here we report a novel cytoplasmic trehalase that hydrolyzes trehalose to glucose. treF, the gene encoding this enzyme, was cloned under ara promoter control. The enzyme (TreF) was purified from extracts of an overexpressing strain and characterized biochemically. It is specific for trehalose exhibiting a Km of 1.9 mM and a Vmax of 54 micromol of trehalose hydrolyzed per min per mg of protein. The enzyme is monomeric, exhibits a broad pH optimum at 6.0, and shows no metal dependency. TreF has a molecular weight of 63,703 (549 amino acids) and is highly homologous to TreA. The nonidentical amino acids of TreF are more polar and more acidic than those of TreA. The expression of treF as studied by the expression of a chromosomal treF-lacZ fusion is weakly induced by high osmolarity of the medium and is partially dependent on RpoS, the stationary-phase sigma factor. Mutants producing 17-fold more TreF than does the wild type were isolated.


This article has been cited by other articles:

  • Cardoso, F. S., Castro, R. F., Borges, N., Santos, H. (2007). Biochemical and genetic characterization of the pathways for trehalose metabolism in Propionibacterium freudenreichii, and their role in stress response. Microbiology 153: 270-280 [Abstract] [Full Text]  
  • Weber, A., Kogl, S. A., Jung, K. (2006). Time-Dependent Proteome Alterations under Osmotic Stress during Aerobic and Anaerobic Growth in Escherichia coli.. J. Bacteriol. 188: 7165-7175 [Abstract] [Full Text]  
  • Higo, A., Katoh, H., Ohmori, K., Ikeuchi, M., Ohmori, M. (2006). The role of a gene cluster for trehalose metabolism in dehydration tolerance of the filamentous cyanobacterium Anabaena sp. PCC 7120.. Microbiology 152: 979-987 [Abstract] [Full Text]  
  • Purvis, J. E., Yomano, L. P., Ingram, L. O. (2005). Enhanced Trehalose Production Improves Growth of Escherichia coli under Osmotic Stress. Appl. Environ. Microbiol. 71: 3761-3769 [Abstract] [Full Text]  
  • Qu, Q., Lee, S.-J., Boos, W. (2004). TreT, a Novel Trehalose Glycosyltransferring Synthase of the Hyperthermophilic Archaeon Thermococcus litoralis. J. Biol. Chem. 279: 47890-47897 [Abstract] [Full Text]  
  • Schluepmann, H., Pellny, T., van Dijken, A., Smeekens, S., Paul, M. (2003). Trehalose 6-phosphate is indispensable for carbohydrate utilization and growth in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 100: 6849-6854 [Abstract] [Full Text]  
  • Berlyn, M. K. B. (1998). Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map. Microbiol. Mol. Biol. Rev. 62: 814-984 [Abstract] [Full Text]  
  • Horlacher, R., Boos, W. (1997). Characterization of TreR, the Major Regulator of the Escherichia coli Trehalose System. J. Biol. Chem. 272: 13026-13032 [Abstract] [Full Text]  
  • Uhland, K., Mondigler, M., Spiess, C., Prinz, W., Ehrmann, M. (2000). Determinants of Translocation and Folding of TreF, a Trehalase of Escherichia coli. J. Biol. Chem. 275: 23439-23445 [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»