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Gene Review

treA  -  periplasmic trehalase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1185, JW1186, osmA
 
 
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Disease relevance of treA

  • The Escherichia coli treA gene encodes an osmotically inducible periplasmic trehalase [1].
  • A 2.5 kb DNA fragment contain a gene encoding a phospho-alpha-(1-1)-glucosidase (phosphotrehalase), designated treA, was isolated from a Bacillus subtilis chromosomal library by complementation of the tre-12 mutation [2].
  • A periplasmic trehalase (alpha,alpha-trehalose glucohydrolase, EC 3.2.1.28) from the thermophilic bacterium Rhodothermus marinus was purified and the respective encoding gene was identified, cloned and overexpressed in Escherichia coli [3].
  • The directions of replication of several prophages integrated with a known orientation in the vicinity of the terminus (tre) of chromosome replication (trp::Mu, min 27; lambda rev integrated within rac, min 31, man::Mu, min 35), have been established by determining the molecular polarity of Okazaki pieces specific to these prophages [4].
 

High impact information on treA

  • Using the in vivo mini-Mu cloning system and growth on trehalose as selection, we cloned the treA gene [5].
  • Minicells containing the treA+ plasmid produced, in addition to three other proteins, the 58,000-dalton protein [5].
  • The 5' flanking region of treA contains an open reading frame which was partially sequenced, whose product shows about 40% identity to sucrose Enzyme II of the phosphotransferase transport system from several organisms [2].
  • These results indicate that treA encodes a specific phospho-alpha-(1-1)-glucosidase which cleaves trehalose-6-phosphate in the cytoplasm after transport and phosphorylation of trehalose [2].
  • As an example of the general utility, we demonstrate treA expression under xylA-operator-promoter control [6].
 

Chemical compound and disease context of treA

 

Biological context of treA

 

Anatomical context of treA

 

Associations of treA with chemical compounds

  • treA and osmY expression and RpoS protein levels were investigated in glucose-limited continuous culture [10].
 

Other interactions of treA

 

Analytical, diagnostic and therapeutic context of treA

References

  1. Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter. Repoila, F., Gutierrez, C. Mol. Microbiol. (1991) [Pubmed]
  2. Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a phospho-alpha-(1-1)-glucosidase encoded by the treA gene. Helfert, C., Gotsche, S., Dahl, M.K. Mol. Microbiol. (1995) [Pubmed]
  3. A highly thermostable trehalase from the thermophilic bacterium Rhodothermus marinus. Jorge, C.D., Sampaio, M.M., Hreggvidsson, G.O., Kristj??nson, J.K., Santos, H. Extremophiles (2007) [Pubmed]
  4. Map position of the replication terminus on the Escherichia coli chromosome. Louarn, J., Patte, J., Louarn, J.M. Mol. Gen. Genet. (1979) [Pubmed]
  5. Trehalase of Escherichia coli. Mapping and cloning of its structural gene and identification of the enzyme as a periplasmic protein induced under high osmolarity growth conditions. Boos, W., Ehmann, U., Bremer, E., Middendorf, A., Postma, P. J. Biol. Chem. (1987) [Pubmed]
  6. Vectors using the phospho-alpha-(1,1)-glucosidase-encoding gene treA of Bacillus subtilis as a reporter. Schöck, F., Gotsche, S., Dahl, M.K. Gene (1996) [Pubmed]
  7. Synthesis, accumulation, and excretion of trehalose in osmotically stressed Escherichia coli K-12 strains: influence of amber suppressors and function of the periplasmic trehalase. Styrvold, O.B., Strøm, A.R. J. Bacteriol. (1991) [Pubmed]
  8. Chromosomal location of gene governing the trehalose utilization in Escherichia coli K12. de Lares, L.B., Ratouchniak, J., Casse, F. Mol. Gen. Genet. (1977) [Pubmed]
  9. Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12. Gutierrez, C., Ardourel, M., Bremer, E., Middendorf, A., Boos, W., Ehmann, U. Mol. Gen. Genet. (1989) [Pubmed]
  10. Induction of RpoS-dependent functions in glucose-limited continuous culture: what level of nutrient limitation induces the stationary phase of Escherichia coli? Notley, L., Ferenci, T. J. Bacteriol. (1996) [Pubmed]
  11. Gene expression of trehalase during post-dormant development of the brine shrimp, Artemia: comparison of the two species. Nambu, Z., Tanaka, S., Nambu, F. J. UOEH (1997) [Pubmed]
  12. Periplasmic trehalase from Escherichia coli--characterization and immobilization on spherisorb. Tourinho-dos-Santos, C.F., Bachinski, N., Paschoalin, V.M., Paiva, C.L., Silva, J.T., Panek, A.D. Braz. J. Med. Biol. Res. (1994) [Pubmed]
 
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