Skip to main content
Log in

TdcA, a transcriptional activator of the tdcABC operon of Escherichia coli, is a member of the LysR family of proteins

  • Original Articles
  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Abstract

The tdcB and tdcC genes of the tdcABC operon of Escherichia coli encode threonine dehydratase and a threonine-serine permease, respectively. These proteins are involved in transport and metabolism of threonine and serine during anaerobic growth. In this study, we functionally characterized tdcA, which encodes a 35 kDa polypeptide consisting of 312 amino acid residues. Non-polar and partially polar mutations introduced into tdcA drastically reduced the expression of the genes down-stream from tdcA. Complementation studies using single-copy chromosomal integrants of a tdcB-lacZ fusion harboring an in-frame deletion of tdcA with chromosomal or plasmid-borne tdcA + in trans showed complete restoration of tdc operon expression in vivo. The amino acid sequene at the amino-terminal end of TdcA revealed a significant homology to the helix-turn-helix motifs of typical DNA binding proteins. Sequence alignment of TdcA with LysR also showed considerable sequence similarity throughout their entire lengths. Our results suggest that TdcA is related to the LysR family of proteins by common ancestry and, based on its functional role in tdc expression, belongs to the LysR family of transcriptional activators.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Datta P, Goss TJ, Omnaas JR, Patil RV (1987) Covalent structure of biodegradative threonine dehydratase of Escherichia coli: homology with other dehydratases. Proc Natl Acad Sci USA 84:393–397

    Google Scholar 

  • Dodd IB, Egan JB (1987) Systematic method for the detection of potential λ cro-like DNA-binding regions in proteins. J Mol Biol 194:557–564

    Google Scholar 

  • Friedman DI, Plantefaber LC, Olson EJ, Carver D, O'Dea MH, Gellert M (1984) Mutations in the DNA gyrB gene that are temperature sensitive for lambda site-specific recombination, Mu growth, and plasmid maintenance. J Bacteriol 157:490–497

    Google Scholar 

  • Goss TJ, Datta P (1985) Molecular cloning and expression of the biodegradative threonine dehydratase gene (tdc) of Escherichia coli. Mol Gen Genet 201:308–314

    Google Scholar 

  • Goss TJ, Schweizer HP, Datta P (1988) Molecular characterization of the tdc operon of Escherichia coli K-12. J Bacteriol 170:5352–5359

    Google Scholar 

  • Green J, Tragesser M, Six S, Unden G, Guest JR (1991) Characterization of the FNR protein of Escherichia coli, an iron-binding transcriptional regulator. Proc R Soc Lond [Biol] 244:137–144

    Google Scholar 

  • Hendrickson W, Schlief RF (1984) Regulation of the Escherichia coli l-arabinose operon studied by gel electrophoresis DNA binding assay. J Mol Biol 174:611–628

    Google Scholar 

  • Henikoff S, Haughn GW, Calvo JM, Wallace JC (1988) A large family of bacterial activator proteins. Proc Natl Acad Sci USA 85:6602–6608

    Google Scholar 

  • Hobert EH, Datta P (1983) Synthesis of biodegradative threonine dehydratase of Escherichia coli: role of amino acids, electron acceptors, and certain intermediary metabolites. J Bacteriol 155:586–592

    Google Scholar 

  • Merberg D, Datta P (1982) Altered expression of biodegradative threonine dehydratase in Escherichia coli mutants. J Bacteriol 150:52–59

    Google Scholar 

  • Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York

    Google Scholar 

  • Pabo CO, Sauer RT (1984) Protein DNA recognition. Annu Rev Biochem 53:293–321

    Google Scholar 

  • Saiki RK, Gelfand DH, Stoffel S, Scharf SJ, Higuchi R, Horn GT, Mullis KB, Erlich HA (1988) Primer directed enzymatic amplification of DNA with thermostable DNA polymerase. Science 239:487–491

    Google Scholar 

  • Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual, 2nd edn, vol 1. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York

    Google Scholar 

  • Sanger F, Nicklen S, Coulson AR (1977) DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74:5463–5467

    Google Scholar 

  • Schweizer HP, Datta, P (1988) Genetic analysis of the tdcABC operon of Escherichia coli K-12. J Bacteriol 170:5360–5363

    Google Scholar 

  • Schweizer HP, Datta P (1989a) Identification and DNA sequence of tdcR, a positive regulatory gene of the tdc operon of Escherichia coli. Mol Gen Genet 218:516–522

    Google Scholar 

  • Schweizer HP, Datta P (1989b) The complete nucleotide sequence of the tdc region of Escherichia coli. Nucleic Acids Res 17:3994

    Google Scholar 

  • Schweizer HP, Datta P (1991) Physical linkage and transcriptional orientation of the tdc operon on the Escherichia coli chromosome. Mol Gen Genet 228:125–128

    Google Scholar 

  • Spiro S, Guest JR (1990) FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol Rev 75:399–428

    Google Scholar 

  • Stragier P, Patte J-C (1983) Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli III Nucleotide sequence and regulation of the LysR gene. J Mol Biol 168:333–350

    Google Scholar 

  • Sumantran VN, Schweizer HP, Datta P (1990) A novel membrane-associated threonine permease encoded by the tdcC gene of Escherichia coli. J Bacteriol 172:428–494

    Google Scholar 

  • Umbarger HE (1978) Amino acid biosynthesis and its regulation. Annu Rev Biochem 47:533–606

    Google Scholar 

  • Vieira J, Messing J (1982) The PUC plasmids, an M13 mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19:259–268

    Google Scholar 

  • Wu Y, Datta P (1992) Integration host factor is required for positive regulation of the tdc operon of Escherichia coli. J Bacteriol 174:233–240

    Google Scholar 

  • Wu, Y, Patil RV, Datta P (1992) Catabolite gene activator protein and integration host factor act in concert to regulate tdc operon expression in Escherichia coli. J Bacteriol 174:6918–6927

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Communicated by H. Hennecke

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ganduri, Y.L., Sadda, S.R., Datta, M.W. et al. TdcA, a transcriptional activator of the tdcABC operon of Escherichia coli, is a member of the LysR family of proteins. Molec. Gen. Genet. 240, 395–402 (1993). https://doi.org/10.1007/BF00280391

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00280391

Key words

Navigation