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Gene Review

glpT  -  sn-glycerol-3-phosphate transporter

Escherichia coli CFT073

 
 
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Disease relevance of glpT

 

High impact information on glpT

 

Chemical compound and disease context of glpT

 

Biological context of glpT

 

Associations of glpT with chemical compounds

  • These mutants did not transport sn-glycerol-3-phosphate, and they lacked GLPT, a protein previously shown to be a product of the glpT operon [1].
  • Both the active phnE and multicopy glpT genes facilitated effective metabolism of low concentrations of DIPP, whereas only the active phnE gene could confer the ability to break down a chromogenic substrate, 5-bromo-4-chloro-3-indoxyl phosphate-p-toluidine (X-Pi) [8].
  • However, nitrate repression on glpT expression was relieved if the upstream region from -290 of the transcription site was removed [11].
  • Furthermore, aerobic expression of glpT was induced by the substrate glycerol 3-phosphate, while the anaerobic expression of glpT was decreased by nitrate, glucose and a fnr mutation [11].
  • DNA micro-array analysis showed that the transcription of glpT and other genes concerning glycerol utilization were highly dependent on the presence of cAMP [6].
 

Other interactions of glpT

  • Analysis of mRNA indicates that glpT and glpQ constitute one operon which is transcribed from a sigma A type promoter [12].
 

Analytical, diagnostic and therapeutic context of glpT

References

  1. A second transport system for sn-glycerol-3-phosphate in Escherichia coli. Argast, M., Ludtke, D., Silhavy, T.J., Boos, W. J. Bacteriol. (1978) [Pubmed]
  2. The transmembrane topology of the sn-glycerol-3-phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusions. Gött, P., Boos, W. Mol. Microbiol. (1988) [Pubmed]
  3. Action at a distance for glp repressor control of glpTQ transcription in Escherichia coli K-12. Yang, B., Gerhardt, S.G., Larson, T.J. Mol. Microbiol. (1997) [Pubmed]
  4. Nucleotide sequence and transcriptional startpoint of the glpT gene of Escherichia coli: extensive sequence homology of the glycerol-3-phosphate transport protein with components of the hexose-6-phosphate transport system. Eiglmeier, K., Boos, W., Cole, S.T. Mol. Microbiol. (1987) [Pubmed]
  5. Emergence of fosfomycin-resistant isolates of Shiga-like toxin-producing Escherichia coli O26. Horii, T., Kimura, T., Sato, K., Shibayama, K., Ohta, M. Antimicrob. Agents Chemother. (1999) [Pubmed]
  6. Fosmidomycin resistance in adenylate cyclase deficient (cya) mutants of Escherichia coli. Sakamoto, Y., Furukawa, S., Ogihara, H., Yamasaki, M. Biosci. Biotechnol. Biochem. (2003) [Pubmed]
  7. sn-Glycerol-3-phosphate transport in Salmonella typhimurium. Hengge, R., Larson, T.J., Boos, W. J. Bacteriol. (1983) [Pubmed]
  8. phnE and glpT genes enhance utilization of organophosphates in Escherichia coli K-12. Elashvili, I., Defrank, J.J., Culotta, V.C. Appl. Environ. Microbiol. (1998) [Pubmed]
  9. Use of Escherichia coli operon-fusion strains for the study of glycerol 3-phosphate transport activity. Miki, K., Lin, E.C. J. Bacteriol. (1980) [Pubmed]
  10. Only one gene is required for the glpT-dependent transport of sn-glycerol-3-phosphate in Escherichia coli. Ludtke, D., Larson, T.J., Beck, C., Boos, W. Mol. Gen. Genet. (1982) [Pubmed]
  11. Transcription of glpT of Escherichia coli K12 is regulated by anaerobiosis and fnr. Wong, K.K., Kwan, H.S. FEMS Microbiol. Lett. (1992) [Pubmed]
  12. The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis. Nilsson, R.P., Beijer, L., Rutberg, B. Microbiology (Reading, Engl.) (1994) [Pubmed]
  13. Divergent transcription of the sn-glycerol-3-phosphate active transport (glpT) and anaerobic sn-glycerol-3-phosphate dehydrogenase (glpA glpC glpB) genes of Escherichia coli K-12. Ehrmann, M., Boos, W., Ormseth, E., Schweizer, H., Larson, T.J. J. Bacteriol. (1987) [Pubmed]
  14. Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Lemieux, M.J., Song, J., Kim, M.J., Huang, Y., Villa, A., Auer, M., Li, X.D., Wang, D.N. Protein Sci. (2003) [Pubmed]
 
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