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Trehalose transport and metabolism in Escherichia coli.
J Bacteriol. 1990 Jun; 172(6):3450-61.JB

Abstract

Trehalose metabolism in Escherichia coli is complicated by the fact that cells grown at high osmolarity synthesize internal trehalose as an osmoprotectant, independent of the carbon source, although trehalose can serve as a carbon source at both high and low osmolarity. The elucidation of the pathway of trehalose metabolism was facilitated by the isolation of mutants defective in the genes encoding transport proteins and degradative enzymes. The analysis of the phenotypes of these mutants and of the reactions catalyzed by the enzymes in vitro allowed the formulation of the degradative pathway at low osmolarity. Thus, trehalose utilization begins with phosphotransferase (IITre/IIIGlc)-mediated uptake delivering trehalose-6-phosphate to the cytoplasm. It continues with hydrolysis to trehalose and proceeds by splitting trehalose, releasing one glucose residue with the simultaneous transfer of the other to a polysaccharide acceptor. The enzyme catalyzing this reaction was named amylotrehalase. Amylotrehalase and EIITre were induced by trehalose in the medium but not at high osmolarity. treC and treB encoding these two enzymes mapped at 96.5 min on the E. coli linkage map but were not located in the same operon. Use of a mutation in trehalose-6-phosphate phosphatase allowed demonstration of the phosphoenolpyruvate- and IITre-dependent in vitro phosphorylation of trehalose. The phenotype of this mutant indicated that trehalose-6-phosphate is the effective in vivo inducer of the system.

Authors+Show Affiliations

Department of Biology, University of Konstanz, Federal Republic of Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

2160944

Citation

Boos, W, et al. "Trehalose Transport and Metabolism in Escherichia Coli." Journal of Bacteriology, vol. 172, no. 6, 1990, pp. 3450-61.
Boos W, Ehmann U, Forkl H, et al. Trehalose transport and metabolism in Escherichia coli. J Bacteriol. 1990;172(6):3450-61.
Boos, W., Ehmann, U., Forkl, H., Klein, W., Rimmele, M., & Postma, P. (1990). Trehalose transport and metabolism in Escherichia coli. Journal of Bacteriology, 172(6), 3450-61.
Boos W, et al. Trehalose Transport and Metabolism in Escherichia Coli. J Bacteriol. 1990;172(6):3450-61. PubMed PMID: 2160944.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Trehalose transport and metabolism in Escherichia coli. AU - Boos,W, AU - Ehmann,U, AU - Forkl,H, AU - Klein,W, AU - Rimmele,M, AU - Postma,P, PY - 1990/6/1/pubmed PY - 1990/6/1/medline PY - 1990/6/1/entrez SP - 3450 EP - 61 JF - Journal of bacteriology JO - J Bacteriol VL - 172 IS - 6 N2 - Trehalose metabolism in Escherichia coli is complicated by the fact that cells grown at high osmolarity synthesize internal trehalose as an osmoprotectant, independent of the carbon source, although trehalose can serve as a carbon source at both high and low osmolarity. The elucidation of the pathway of trehalose metabolism was facilitated by the isolation of mutants defective in the genes encoding transport proteins and degradative enzymes. The analysis of the phenotypes of these mutants and of the reactions catalyzed by the enzymes in vitro allowed the formulation of the degradative pathway at low osmolarity. Thus, trehalose utilization begins with phosphotransferase (IITre/IIIGlc)-mediated uptake delivering trehalose-6-phosphate to the cytoplasm. It continues with hydrolysis to trehalose and proceeds by splitting trehalose, releasing one glucose residue with the simultaneous transfer of the other to a polysaccharide acceptor. The enzyme catalyzing this reaction was named amylotrehalase. Amylotrehalase and EIITre were induced by trehalose in the medium but not at high osmolarity. treC and treB encoding these two enzymes mapped at 96.5 min on the E. coli linkage map but were not located in the same operon. Use of a mutation in trehalose-6-phosphate phosphatase allowed demonstration of the phosphoenolpyruvate- and IITre-dependent in vitro phosphorylation of trehalose. The phenotype of this mutant indicated that trehalose-6-phosphate is the effective in vivo inducer of the system. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/2160944/Trehalose_transport_and_metabolism_in_Escherichia_coli_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=2160944 DB - PRIME DP - Unbound Medicine ER -