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Gene Review

TRP3  -  bifunctional anthranilate synthase/indole...

Saccharomyces cerevisiae S288c

Synonyms: Multifunctional tryptophan biosynthesis protein, YKL211C
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Disease relevance of TRP3


High impact information on TRP3

  • Using his3 as an internal standard, the number of mRNA molecules per cell have been determined for ded1, trp3, rps4, and gall under a variety of growth conditions [2].
  • Analysis of a number of peptides obtained by this selection procedure indicates that Trp1, Trp3, Pro8, and Gly9 are important for agonist activity specifically [3].
  • Transcription of the TRP3 gene of Saccharomyces cerevisiae is regulated by GCN4p from a position proximal to the transcriptional initiation sites [4].
  • GCN4p activation of the yeast TRP3 gene is enhanced by ABF1p and uses a suboptimal TATA element [4].
  • According to the kinetic parameters of the purified isomerase protein, the enzyme is more active than, for example, the purified TRP3 enzyme indoleglycerol-phosphate synthase [5].

Biological context of TRP3

  • The nucleotide sequence of TRP2 as well as that of TRP3 were determined [6].
  • The 9 base pair direct repeat (Hinnebusch, A.G., and Fink, G.R. (1983) J. Biol. Chem. 258, 5238-5247) and inverted repeats were identified in the 5'-flanking sequences of TRP2 and TRP3 [6].
  • Genetic mapping by tetrad analysis shows that the SPE1 gene is located on the left arm of chromosome XI, 6 cM from the LAP1 gene and 43 cM from the TRP3 gene [7].
  • In addition, we show by random-breakage mapping that TRP3 is located approximately 45 kb from the left telomere of chromosome XI, whereas FAS1 is approximately 110 kb from the same telomere [8].
  • Analogous reorganization was also observed with respect to integrative plasmids carrying the TRP3 and HIS3 genes of H. polymorpha and the ADE2 gene of Saccharomyces cerevisiae as selectable markers [9].

Associations of TRP3 with chemical compounds

  • Saccharomyces cerevisiae anthranilate synthase:indole-3-glycerol phosphate synthase is a multifunctional hetero-oligomeric enzyme encoded by genes TRP2 and TRP3 [6].
  • No significant differences in the doubling times of TRP3 or TRP3pr yeast transformants were observed during growth at 25 degrees C, 30 degrees C or 37 degrees C, or in the presence of sublethal concentrations of the analogue, 5-methyltryptophan [10].
  • However, fusion of SUMO to the N-terminus of Gcn5 to mimic constitutive sumoylation resulted in defective growth on 3-aminotriazole media and reduced basal and activated transcription of the SAGA-dependent gene TRP3 [11].
  • However, such modifications that weaken the interaction with phospholipid bilayer (deletion of Trp1 and substitution of Trp3 by Gly or Ala) appreciably lower the physiological activity [12].
  • The interaction of the side chains of Trp1 and Trp3 residues of alpha-mating factor with the hydrophobic interior of the bilayer contributes to the binding of this peptide with the phosphatidylcholine bilayer [12].

Other interactions of TRP3

  • Therefore, the steady state amount of TRP1 mRNA in yeast cells, grown without amino acid limitation, is similar to the steady-state amount of TRP3 mRNA [5].
  • The TRP3pr gene was able to complement a trp3:: URA3 null mutation in yeast [10].
  • Orientation of enzymic domains in tryptophan synthase of Neurospora crassa: an immunoblot analysis of TRP3 mutant products [13].
  • These results indicate that the position 7 side-chain is likely interacting with a pocket formed by extracellular domains of Ste2p, whereas the side-chain of Trp3 is in a hydrophobic pocket possibly within the transmembrane region of the receptor [14].


  1. The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase. Crombie, T., Boyle, J.P., Coggins, J.R., Brown, A.J. Eur. J. Biochem. (1994) [Pubmed]
  2. Absolute mRNA levels and transcriptional initiation rates in Saccharomyces cerevisiae. Iyer, V., Struhl, K. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  3. Yeast alpha mating factor structure-activity relationship derived from genetically selected peptide agonists and antagonists of Ste2p. Manfredi, J.P., Klein, C., Herrero, J.J., Byrd, D.R., Trueheart, J., Wiesler, W.T., Fowlkes, D.M., Broach, J.R. Mol. Cell. Biol. (1996) [Pubmed]
  4. GCN4p activation of the yeast TRP3 gene is enhanced by ABF1p and uses a suboptimal TATA element. Martens, J.A., Brandl, C.J. J. Biol. Chem. (1994) [Pubmed]
  5. The role of the TRP1 gene in yeast tryptophan biosynthesis. Braus, G.H., Luger, K., Paravicini, G., Schmidheini, T., Kirschner, K., Hütter, R. J. Biol. Chem. (1988) [Pubmed]
  6. 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]
  7. Ornithine decarboxylase in Saccharomyces cerevisiae: chromosomal assignment and genetic mapping of the SPE1 gene. Xie, Q.W., Tabor, C.W., Tabor, H. Yeast (1990) [Pubmed]
  8. The use of random-breakage mapping to locate the genes APN1 and YUH1 in the Saccharomyces genome, and to determine gene order near the left end of chromosome XI. Game, J., Bell, M., Ramotar, D., Miller, H. Yeast (1994) [Pubmed]
  9. Plasmid reorganization during integrative transformation in Hansenula polymorpha. Bogdanova, A.I., Agaphonov, M.O., Ter-Avanesyan, M.D. Yeast (1995) [Pubmed]
  10. Protein folding within the cell is influenced by controlled rates of polypeptide elongation. Crombie, T., Swaffield, J.C., Brown, A.J. J. Mol. Biol. (1992) [Pubmed]
  11. Sumoylation of the yeast Gcn5 protein. Sterner, D.E., Nathan, D., Reindle, A., Johnson, E.S., Berger, S.L. Biochemistry (2006) [Pubmed]
  12. Conformations of yeast alpha-mating factor and analog peptides as bound to phospholipid bilayer. Correlation of membrane-bound conformation with physiological activity. Wakamatsu, K., Okada, A., Miyazawa, T., Masui, Y., Sakakibara, S., Higashijima, T. Eur. J. Biochem. (1987) [Pubmed]
  13. Orientation of enzymic domains in tryptophan synthase of Neurospora crassa: an immunoblot analysis of TRP3 mutant products. Matchett, W.H., Lacy, A.M., DeMoss, J.A. Mol. Gen. Genet. (1987) [Pubmed]
  14. Study of the binding environment of alpha-factor in its G protein-coupled receptor using fluorescence spectroscopy. Ding, F.X., Lee, B.K., Hauser, M., Patri, R., Arshava, B., Becker, J.M., Naider, F. J. Pept. Res. (2002) [Pubmed]
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