Literature DB >> 8449875

Induction of the lambda receptor is essential for effective uptake of trehalose in Escherichia coli.

W Klein1, W Boos.   

Abstract

Trehalose transport in Escherichia coli after growth at low osmolarity is mediated by enzyme IITre of the phosphotransferase system (W. Boos, U. Ehmann, H. Forkl, W. Klein, M. Rimmele, and P. Postma, J. Bacteriol. 172:3450-3461, 1990). The apparent Km (16 microM) of trehalose uptake is low. Since trehalose is a good source of carbon and the apparent affinity of the uptake system is high, it was surprising that the disaccharide trehalose [O-alpha-D-glucosyl(1-1)-alpha-D-glucoside] has no problems diffusing through the outer membrane at high enough rates to allow full growth, particularly at low substrate concentrations. Here we show that induction of the maltose regulon is required for efficient utilization of trehalose. malT mutants that lack expression of all maltose genes, as well as lamB mutants that lack only the lambda receptor (maltoporin), still grow on trehalose at the usual high (10 mM) trehalose concentrations in agar plates, but they exhibit the half-maximal rate of trehalose uptake at concentrations that are 50-fold higher than in the wild-type (malT+) strain. The maltose system is induced by trehalose to about 30% of the fully induced level reached when grown in the presence of maltose in a malT+ strain or when grown on glycerol in a maltose-constitutive strain [malT(Con)]. The 30% level of maximal expression is sufficient for maximal trehalose utilization, since there is no difference in the concentration of trehalose required for the half-maximal rate of uptake in trehalose-grown strains with the wild-type gene (malT+) or with strains constitutive for the maltose system [malT(Con)]. In contrast, when the expression of the lambda receptor is reduced to less than 20% of the maximal level, trehalose uptake becomes less efficient. Induction of the maltose system by trehalose requires metabolism of trehalose. Mutants lacking amylotrehalase, the key enzyme in trehalose utilization, accumulate trehalose but do not induce the maltose system.

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Year:  1993        PMID: 8449875      PMCID: PMC203962          DOI: 10.1128/jb.175.6.1682-1686.1993

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  35 in total

1.  Periplasmic protein related to the sn-glycerol-3-phosphate transport system of Escherichia coli.

Authors:  T J Silhavy; I Hartig-Beecken; W Boos
Journal:  J Bacteriol       Date:  1976-05       Impact factor: 3.490

2.  [Existence in Escherichia coli K 12 of a common regulation of the biosynthesis of bacteriophage receptors and maltose metabolism].

Authors:  M Schwartz
Journal:  Ann Inst Pasteur (Paris)       Date:  1967-11

3.  Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor.

Authors:  S Szmelcman; M Hofnung
Journal:  J Bacteriol       Date:  1975-10       Impact factor: 3.490

4.  Positive selection for loss of tetracycline resistance.

Authors:  B R Bochner; H C Huang; G L Schieven; B N Ames
Journal:  J Bacteriol       Date:  1980-08       Impact factor: 3.490

Review 5.  Maltose and lactose transport in Escherichia coli. Examples of two different types of concentrative transport systems.

Authors:  R Hengge; W Boos
Journal:  Biochim Biophys Acta       Date:  1983-08-11

6.  Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein.

Authors:  O Kellermann; S Szmelcman
Journal:  Eur J Biochem       Date:  1974-08-15

7.  Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching.

Authors:  S Szmelcman; M Schwartz; T J Silhavy; W Boos
Journal:  Eur J Biochem       Date:  1976-05-17

8.  Investigation of the selectivity of maltoporin channels using mutant LamB proteins: mutations changing the maltodextrin binding site.

Authors:  R Benz; G Francis; T Nakae; T Ferenci
Journal:  Biochim Biophys Acta       Date:  1992-03-02

9.  The action pattern of amylomaltase from Escherichia coli.

Authors:  T N Palmer; B E Ryman; W J Whelan
Journal:  Eur J Biochem       Date:  1976-10-01

10.  Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrins and starch polysaccharides.

Authors:  T Ferenci; M Schwentorat; S Ullrich; J Vilmart
Journal:  J Bacteriol       Date:  1980-05       Impact factor: 3.490

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  11 in total

1.  The maltodextrin system of Escherichia coli: glycogen-derived endogenous induction and osmoregulation.

Authors:  Renate Dippel; Tobias Bergmiller; Alex Böhm; Winfried Boos
Journal:  J Bacteriol       Date:  2005-12       Impact factor: 3.490

2.  Long-term experimental evolution in Escherichia coli. IV. Targets of selection and the specificity of adaptation.

Authors:  M Travisano; R E Lenski
Journal:  Genetics       Date:  1996-05       Impact factor: 4.562

3.  High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis.

Authors:  K B Xavier; L O Martins; R Peist; M Kossmann; W Boos; H Santos
Journal:  J Bacteriol       Date:  1996-08       Impact factor: 3.490

4.  Molecular characterization of glucokinase from Escherichia coli K-12.

Authors:  D Meyer; C Schneider-Fresenius; R Horlacher; R Peist; W Boos
Journal:  J Bacteriol       Date:  1997-02       Impact factor: 3.490

5.  Identification of a new porin, RafY, encoded by raffinose plasmid pRSD2 of Escherichia coli.

Authors:  C Ulmke; J W Lengeler; K Schmid
Journal:  J Bacteriol       Date:  1997-09       Impact factor: 3.490

Review 6.  Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation.

Authors:  W Boos; H Shuman
Journal:  Microbiol Mol Biol Rev       Date:  1998-03       Impact factor: 11.056

7.  Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system.

Authors:  K Decker; R Peist; J Reidl; M Kossmann; B Brand; W Boos
Journal:  J Bacteriol       Date:  1993-09       Impact factor: 3.490

8.  The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa.

Authors:  J L Wylie; E A Worobec
Journal:  J Bacteriol       Date:  1995-06       Impact factor: 3.490

9.  Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose.

Authors:  W Klein; R Horlacher; W Boos
Journal:  J Bacteriol       Date:  1995-07       Impact factor: 3.490

10.  Compensatory evolution of gene regulation in response to stress by Escherichia coli lacking RpoS.

Authors:  Daniel M Stoebel; Karsten Hokamp; Michael S Last; Charles J Dorman
Journal:  PLoS Genet       Date:  2009-10-02       Impact factor: 5.917

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