The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

trpC  -  indole-3-glycerolphosphate synthetase and...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1256, JW1254, trpF
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of trpC


High impact information on trpC


Chemical compound and disease context of trpC


Biological context of trpC


Associations of trpC with chemical compounds

  • These genes encode two bifunctional proteins thought to have arisen by gene fusions: the trpD polypeptide contains the glutamine amido transferase and the phosphoribosyl anthranilate transferase activities, and the trpC protein possesses the N-(5'-phosphoribosyl)-anthranilic acid isomerase and the indole-3-glycerol phosphate synthetase activities [2].
  • To obtain a better understanding of this sluggishness, we used DNA shuffling to mutagenize the trpC gene, which encodes indoleglycerol phosphate synthase, from the hyperthermophile Sulfolobus solfataricus [13].
  • Phosphoribosylanthranilate (PRA) isomerase activity, which is also carried by the trpC protein, is unstable during starvation for ammonium, cysteine, or sulfate but is stable under other nongrowing conditions where InGP synthetase is not [14].

Regulatory relationships of trpC

  • The plasmid pAJ24JI suppressed trpA, B and F mutants, pAJ73JI suppressed trpC and D and pAJ88JI suppressed a trpE mutant [15].

Other interactions of trpC

  • The products of the operator-distal structural genes trpC, trpB, and trpA are formed at rates approximately 15-fold higher than those of wild type [16].
  • High-level expression of TrpC-TonB protein in the absence of tryptophan results in virtually immediate cessation of growth for strains carrying the trpC-tonB plasmid [17].
  • An amdS320 strain was transformed to AmdS+ and cotransformed with a DNA fragment containing a fusion between a non-functional A. nidulans trpC gene and the Escherichia coli lacZ gene [18].
  • We have shown that the Aspergillus nidulans ans1 sequence enhances the efficiency of transformation when introduced into vectors containing argB or trpC genes [19].

Analytical, diagnostic and therapeutic context of trpC

  • Southern blot analysis of DNA from these Trp+ transformants showed that plasmid DNA was present but that this DNA was not integrated at the site of the chromosomal trpC locus [20].
  • The A. niger trpC gene was localized on the cloned fragment by heterologous hybridization experiments and sequence analysis [20].
  • The utility of this "instant gene bank" technique is demonstrated here by the molecular cloning of the P. canescens trpC gene [21].


  1. Tryptophan auxotrophic mutants in Aspergillus niger: inactivation of the trpC gene by cotransformation mutagenesis. Goosen, T., van Engelenburg, F., Debets, F., Swart, K., Bos, K., van den Broek, H. Mol. Gen. Genet. (1989) [Pubmed]
  2. Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium. Horowitz, H., Van Arsdell, J., Platt, T. J. Mol. Biol. (1983) [Pubmed]
  3. Developmental regulation of the Aspergillus nidulans trpC gene. Yelton, M.M., Hamer, J.E., de Souza, E.R., Mullaney, E.J., Timberlake, W.E. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  4. Tryptophan biosynthesis genes trpEGC in the thermoacidophilic archaebacterium Sulfolobus solfataricus. Tutino, M.L., Scarano, G., Marino, G., Sannia, G., Cubellis, M.V. J. Bacteriol. (1993) [Pubmed]
  5. The sequence of a symbiotically essential Bradyrhizobium japonicum operon consisting of trpD, trpC and a moaC-like gene. Kuykendall, L.D., Hunter, W.J. Biochim. Biophys. Acta (1997) [Pubmed]
  6. A secondary attachment site for bacteriophage lambda in trpC of E. coli. Christie, G.E., Platt, T. Cell (1979) [Pubmed]
  7. Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 and TRP3 encoding bifunctional anthranilate synthase: indole-3-glycerol phosphate synthase. Zalkin, H., Paluh, J.L., van Cleemput, M., Moye, W.S., Yanofsky, C. J. Biol. Chem. (1984) [Pubmed]
  8. Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions. Christie, G.E., Platt, T. J. Mol. Biol. (1980) [Pubmed]
  9. Efficient integrative transformation of the phytopathogenic fungus Alternaria alternata mediated by the repetitive rDNA sequences. Tsuge, T., Nishimura, S., Kobayashi, H. Gene (1990) [Pubmed]
  10. Expression of Escherichia coli trp genes and the mouse dihydrofolate reductase gene cloned in Bacillus subtilis. Williams, D.M., Schoner, R.G., Duvall, E.J., Preis, L.H., Lovett, P.S. Gene (1981) [Pubmed]
  11. Translational coupling during expression of the tryptophan operon of Escherichia coli. Oppenheim, D.S., Yanofsky, C. Genetics (1980) [Pubmed]
  12. The structure of the trpE, trpD and 5' trpC genes of Bacillus pumilus. Rivas, M.V., Jarvis, E.D., Rudner, R. Gene (1990) [Pubmed]
  13. Improving the catalytic activity of a thermophilic enzyme at low temperatures. Merz, A., Yee, M.C., Szadkowski, H., Pappenberger, G., Crameri, A., Stemmer, W.P., Yanofsky, C., Kirschner, K. Biochemistry (2000) [Pubmed]
  14. Inactivation and partial degradation of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase in nongrowing cultures of Escherichia coli. Mosteller, R.D., Nishimoto, K.R., Goldstein, R.V. J. Bacteriol. (1977) [Pubmed]
  15. Tryptophan genes in Rhizobium--their organization and their transfer to other bacterial genera. Johnston, A.W., Bibb, M.J., Beringer, J.E. Mol. Gen. Genet. (1978) [Pubmed]
  16. Isolation and characterization of mutations creating high-efficiency transcription initiation signals within the trp operon of Escherichia coli. McPartland, A., Somerville, R.L. J. Bacteriol. (1976) [Pubmed]
  17. A mutation in the amino terminus of a hybrid TrpC-TonB protein relieves overproduction lethality and results in cytoplasmic accumulation. Skare, J.T., Roof, S.K., Postle, K. J. Bacteriol. (1989) [Pubmed]
  18. Cotransformation of Aspergillus nidulans: a tool for replacing fungal genes. Wernars, K., Goosen, T., Wennekes, B.M., Swart, K., van den Hondel, C.A., van den Broek, H.W. Mol. Gen. Genet. (1987) [Pubmed]
  19. Enhancement of Aspergillus nidulans transformation by the ans1 sequence. Dzikowska, A., Wegleński, P. Acta Microbiol. Pol. (1989) [Pubmed]
  20. Isolation and characterization of the Aspergillus niger trpC gene. Kos, A., Kuijvenhoven, J., Wernars, K., Bos, C.J., van den Broek, H.W., Pouwels, P.H., van den Hondel, C.A. Gene (1985) [Pubmed]
  21. An 'instant gene bank' method for gene cloning by mutant complementation. Gems, D., Aleksenko, A., Belenky, L., Robertson, S., Ramsden, M., Vinetski, Y., Clutterbuck, A.J. Mol. Gen. Genet. (1994) [Pubmed]
WikiGenes - Universities