Summary
The structure and function of the TRP3 gene of Saccharomyces cerevisiae were analyzed. Subcloning of an original 4.8 kb BamHI DNA fragment, carrying the yeast TRP3 gene, allowed for a localization of the gene on a 2.5 kb ClaI/BamHI fragment. Transcription was found to proceed from the ClaI site towards the BamHI site. Three major transcription start sites were determined at positions −92, −87, and −81 by S1-mapping. The synthesis of the TRP3 gene is regulated by the general control, and was found to take place- at the transcriptional level. The sequence of the 5′-noncoding region up to position −400 and part of the coding region to position 840 were determined. The 5′-noncoding region contains sequences common to most amino acid biosynthetic genes known so far, namely a presumptive ribosome binding site, “Goldberg-Hogness boxes”, and a consensus sequence, possibly involved in the general control. For the coding region a single open reading frame was found. The deduced amino acid sequence was aligned with homologous amino acid sequences of Neurospora crassa, Pseudomonas putida and Escherichia coli. The exceptionally high homology (40–60%) between these sequences led us to postulate that the TRP3 gene product is of the structure NH2-glutamine amidotransferase-indole-3-glycerol-phosphate synthase-COOH.
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References
Aebi M, Niederberger P, Hütter R (1982) Curr Genet 5:39–46
Andreadis A, Yun-Pung H, Kohlhaw GB, Schimmel P, (1982) Cell 31:319–325
Aviv H, Leder P (1972) Proc Natl Acad Sci USA 69:1408–1412
Bantle JA, Maxwell IH, Hahn WE (1976) Anal Biochem 72:413–427
Bennetzen JL, Hall BD (1982) J Biol Chem 257:3018–3025
Berk AJ, Sharp PA (1977) Cell 12:721–732
Casey J, Davidson N (1977) Nucleic Acids Res 4:1539–1552
Dobson MJ, Tuite ME, Roberts NA, Kingsman AJ, Kingsman SM (1982) Nucleic Acids Res 10:2625–2637
Dobson MJ, Tuite MF, Mellor J, Roberts NA, King RM, Burke DC, Kingsman AJ, Kingsman SM (1983) Nucleic Acids Res 11:2289–2302
Donahue TF, Farabough PJ, Fink GR (1982) Gene 18:47–59
Donahue TF, Daves RS, Lucchini G, Fink GR (1983) Cell 32:89–98
Faye G, Leung DW, Tatchel K, Hall BD, Smith M (1981) Proc Natl Acad Sci USA 78:2258–2262
Hinnebusch AG, Fink GR (1983) J Biol Chem 258:5238–5247
Hsiao C, Carbon C (1979) Proc Natl Acad Sci USA 76:3829–3833
Hütter R, DeMoss JA (1967a) Genetics 55:241–247
Hütter R, DeMoss JA (1967b) J Bacteriol 94:1896–1907
Kawamura M, Klein PS, Goto Y, Zalkin H, Hendrikson RL (1978) J Biol Chem 253:4659–4668
Kozak M (1978) Cell 15:1109–1123
Kozak M (1981) Nucleic Acids Res 9:5233–5252
Landolt-Sydler M-Y (1974) Arch Genet 47:65–85
Maxam A, Gilbert W (1980) Methods Enzymol 65:499–560
McDonell MW, Simon MN, Studier WF (1977) J Mol Biol 110:119–146
McKnight SL, Kingsbury R (1982) Science 217:316–324
Miozzari G, Niederberger P, Hütter R (1978) J Bacteriol 134:48–59
Mortimer RK, Hawthorne DC (1966) Genetics 53:165–173
Niederberger P, Miozzari G, Hütter R (1981) Mol Cell Biol 1:584–593
Philippsen P, Thomas M, Kramer RA, Davis RW (1978) J Mol Biol 123:387–404
Rave N, Crkvenjaker R, Boedtker H (1979) Nucleic Acids Res 6:3559–3567
Rigby PWJ, Dieckmann M, Rhodes C, Berg P (1977) J Mol Biol 113:237–251
Rubtov PM, Musakhanov MM, Zakharyev VM, Kramer AS, Skryabin KG, Bayer AA (1980) Nucleic Acids Res 8:5779–5812
Schechtman MG, Yanofsky C (1983) J Mol Appl Genet 2:83–99
Schürch-Rathgeb Y (1972) Arch Genet 45:129–192
Sherman F, Fink GR, Lukins HB (1970) Methods in Yeast Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
Struhl K (1982) Proc Natl Acad Sci USA 79:7385–7389
Tabak HF, Flavell RA (1978) Nucleic Acids Res 5:2321–2332
Tabak HIT, Hecht NB, Menke HH, Hollenberg CP (1979) Curr Genet 1:33–43
Thomas PS (1980) Proc Natl Acad Sci USA 77:5201–5205
Thuriaux P, Heyer W -D, Strauss A (1982) Curr Genet 6:13–18
Tschumper G, Carbon J (1980) Gene 10:157–166
Wahl GM, Stern M, Stark GR (1979) Proc Natl Acad Sci USA 76:3683–3687
Weaver RF, Weissmann C (1979) Nucleic Acids Res 5:1175–1193
Yanofsky C, Platt T, Crawford JP, Nichols BP, Christie GE, Horowitz H, van Cleemput M, Wu AM (1981) Nucleic Acids Res 9:6647–6668
Zalkin H, Yanofsky C (1982) J Biol Chem 257:1491–1500
Zitomer RS, Hall BD (1976) J Biol Chem 251:6320–6326
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Aebi, M., Furter, R., Prand, F. et al. Structure and function of the TRP3 gene of Saccharomyces cerevisiae: Analysis of transcription, promoter sequence, and sequence coding for a glutamine amidotransferase. Curr Genet 8, 165–172 (1984). https://doi.org/10.1007/BF00417812
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DOI: https://doi.org/10.1007/BF00417812