Abstract
The Saccharomyces cerevisiae PHO4 gene, which positively controls the expression of phosphatase genes, has been isolated by complementation of a pho4 mutation. The isolated DNA directed integration at the chromosomal PHO4 locus. The nucleotide sequence of PHO4 has a coding region of 930 nucleotides, flanked by sequences with typical transcription initiation and termination signals. The 5' region has characteristics of low-expression promoters and carries several uncommon elements, whose significance is not known. The predicted primary structure of the PHO4 protein, of 309 residues, does not show sequence elements typical of DNA-binding proteins. The transcription of PHO4 is independent of inorganic phosphate. Like other regulatory genes, PHO4 is transcribed at a very low level and the translation of its message uses preferentially several codons which are not employed for highly expressed genes.
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Selected References
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- Arima K., Oshima T., Kubota I., Nakamura N., Mizunaga T., Toh-e A. The nucleotide sequence of the yeast PHO5 gene: a putative precursor of repressible acid phosphatase contains a signal peptide. Nucleic Acids Res. 1983 Mar 25;11(6):1657–1672. doi: 10.1093/nar/11.6.1657. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bajwa W., Meyhack B., Rudolph H., Schweingruber A. M., Hinnen A. Structural analysis of the two tandemly repeated acid phosphatase genes in yeast. Nucleic Acids Res. 1984 Oct 25;12(20):7721–7739. doi: 10.1093/nar/12.20.7721. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bennetzen J. L., Hall B. D. The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase. J Biol Chem. 1982 Mar 25;257(6):3018–3025. [PubMed] [Google Scholar]
- Bostian K. A., Lemire J. M., Cannon L. E., Halvorson H. O. In vitro synthesis of repressible yeast acid phosphatase: identification of multiple mRNAs and products. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4504–4508. doi: 10.1073/pnas.77.8.4504. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bostian K. A., Lemire J. M., Halvorson H. O. Physiological control of repressible acid phosphatase gene transcripts in Saccharomyces cerevisiae. Mol Cell Biol. 1983 May;3(5):839–853. doi: 10.1128/mcb.3.5.839. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bram R. J., Kornberg R. D. Specific protein binding to far upstream activating sequences in polymerase II promoters. Proc Natl Acad Sci U S A. 1985 Jan;82(1):43–47. doi: 10.1073/pnas.82.1.43. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brent R. Repression of transcription in yeast. Cell. 1985 Aug;42(1):3–4. doi: 10.1016/s0092-8674(85)80091-x. [DOI] [PubMed] [Google Scholar]
- Burke R. L., Tekamp-Olson P., Najarian R. The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae. J Biol Chem. 1983 Feb 25;258(4):2193–2201. [PubMed] [Google Scholar]
- Chevallier M. R., Bloch J. C., Lacroute F. Transcriptional and translational expression of a chimeric bacterial-yeast plasmid in yeasts. Gene. 1980 Oct;11(1-2):11–19. doi: 10.1016/0378-1119(80)90082-7. [DOI] [PubMed] [Google Scholar]
- DORN G. GENETIC ANALYSIS OF THE PHOSPHATASES IN ASPERGILLUS NIDULANS. Genet Res. 1965 Feb;6:13–26. doi: 10.1017/s0016672300003943. [DOI] [PubMed] [Google Scholar]
- Dobson M. J., Tuite M. F., Roberts N. A., Kingsman A. J., Kingsman S. M., Perkins R. E., Conroy S. C., Fothergill L. A. Conservation of high efficiency promoter sequences in Saccharomyces cerevisiae. Nucleic Acids Res. 1982 Apr 24;10(8):2625–2637. doi: 10.1093/nar/10.8.2625. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Elder R. T., Loh E. Y., Davis R. W. RNA from the yeast transposable element Ty1 has both ends in the direct repeats, a structure similar to retrovirus RNA. Proc Natl Acad Sci U S A. 1983 May;80(9):2432–2436. doi: 10.1073/pnas.80.9.2432. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fraser R. S. Turnover of polyadenylated messenger RNA in fission yeast. Evidence for the control of protein synthesis at the translational level. Eur J Biochem. 1975 Dec 15;60(2):477–486. doi: 10.1111/j.1432-1033.1975.tb21026.x. [DOI] [PubMed] [Google Scholar]
- Giniger E., Varnum S. M., Ptashne M. Specific DNA binding of GAL4, a positive regulatory protein of yeast. Cell. 1985 Apr;40(4):767–774. doi: 10.1016/0092-8674(85)90336-8. [DOI] [PubMed] [Google Scholar]
- Godson G. N., Vapnek D. A simple method of preparing large amounts of phiX174 RF 1 supercoiled DNA. Biochim Biophys Acta. 1973 Apr 11;299(4):516–520. doi: 10.1016/0005-2787(73)90223-2. [DOI] [PubMed] [Google Scholar]
- Guarente L. Yeast promoters: positive and negative elements. Cell. 1984 Apr;36(4):799–800. doi: 10.1016/0092-8674(84)90028-x. [DOI] [PubMed] [Google Scholar]
- Hall M. N., Hereford L., Herskowitz I. Targeting of E. coli beta-galactosidase to the nucleus in yeast. Cell. 1984 Apr;36(4):1057–1065. doi: 10.1016/0092-8674(84)90055-2. [DOI] [PubMed] [Google Scholar]
- Heidecker G., Messing J., Gronenborn B. A versatile primer for DNA sequencing in the M13mp2 cloning system. Gene. 1980 Jun;10(1):69–73. doi: 10.1016/0378-1119(80)90145-6. [DOI] [PubMed] [Google Scholar]
- Henikoff S., Kelly J. D., Cohen E. H. Transcription terminates in yeast distal to a control sequence. Cell. 1983 Jun;33(2):607–614. doi: 10.1016/0092-8674(83)90441-5. [DOI] [PubMed] [Google Scholar]
- Hicks J. B., Hinnen A., Fink G. R. Properties of yeast transformation. Cold Spring Harb Symp Quant Biol. 1979;43(Pt 2):1305–1313. doi: 10.1101/sqb.1979.043.01.149. [DOI] [PubMed] [Google Scholar]
- Hinnen A., Hicks J. B., Fink G. R. Transformation of yeast. Proc Natl Acad Sci U S A. 1978 Apr;75(4):1929–1933. doi: 10.1073/pnas.75.4.1929. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hope I. A., Struhl K. GCN4 protein, synthesized in vitro, binds HIS3 regulatory sequences: implications for general control of amino acid biosynthetic genes in yeast. Cell. 1985 Nov;43(1):177–188. doi: 10.1016/0092-8674(85)90022-4. [DOI] [PubMed] [Google Scholar]
- Kammerer B., Guyonvarch A., Hubert J. C. Yeast regulatory gene PPR1. I. Nucleotide sequence, restriction map and codon usage. J Mol Biol. 1984 Dec 5;180(2):239–250. doi: 10.1016/s0022-2836(84)80002-9. [DOI] [PubMed] [Google Scholar]
- Kozak M. Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes. Nucleic Acids Res. 1981 Oct 24;9(20):5233–5252. doi: 10.1093/nar/9.20.5233. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kramer R. A., Andersen N. Isolation of yeast genes with mRNA levels controlled by phosphate concentration. Proc Natl Acad Sci U S A. 1980 Nov;77(11):6541–6545. doi: 10.1073/pnas.77.11.6541. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laughon A., Gesteland R. F. Primary structure of the Saccharomyces cerevisiae GAL4 gene. Mol Cell Biol. 1984 Feb;4(2):260–267. doi: 10.1128/mcb.4.2.260. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lemire J. M., Willcocks T., Halvorson H. O., Bostian K. A. Regulation of repressible acid phosphatase gene transcription in Saccharomyces cerevisiae. Mol Cell Biol. 1985 Aug;5(8):2131–2141. doi: 10.1128/mcb.5.8.2131. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Messenguy F. Regulation of arginine biosynthesis in Saccharomyces cerevisiae: isolation of a cis-dominant, constitutive mutant for ornithine carbamoyltransferase synthesis. J Bacteriol. 1976 Oct;128(1):49–55. doi: 10.1128/jb.128.1.49-55.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
- Meyhack B., Bajwa W., Rudolph H., Hinnen A. Two yeast acid phosphatase structural genes are the result of a tandem duplication and show different degrees of homology in their promoter and coding sequences. EMBO J. 1982;1(6):675–680. doi: 10.1002/j.1460-2075.1982.tb01229.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Moreland R. B., Nam H. G., Hereford L. M., Fried H. M. Identification of a nuclear localization signal of a yeast ribosomal protein. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6561–6565. doi: 10.1073/pnas.82.19.6561. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Norrander J., Kempe T., Messing J. Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene. 1983 Dec;26(1):101–106. doi: 10.1016/0378-1119(83)90040-9. [DOI] [PubMed] [Google Scholar]
- Petes T. D., Broach J. R., Wensink P. C., Hereford L. M., Fink G. R., Botstein D. Isolation and analysis of recombinant DNA molecules containing yeast DNA. Gene. 1978 Sep;4(1):37–49. doi: 10.1016/0378-1119(78)90013-6. [DOI] [PubMed] [Google Scholar]
- Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
- Rogers D. T., Lemire J. M., Bostian K. A. Acid phosphatase polypeptides in Saccharomyces cerevisiae are encoded by a differentially regulated multigene family. Proc Natl Acad Sci U S A. 1982 Apr;79(7):2157–2161. doi: 10.1073/pnas.79.7.2157. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Silver P. A., Keegan L. P., Ptashne M. Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization. Proc Natl Acad Sci U S A. 1984 Oct;81(19):5951–5955. doi: 10.1073/pnas.81.19.5951. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stiles J. I., Szostak J. W., Young A. T., Wu R., Consaul S., Sherman F. DNA sequence of a mutation in the leader region of the yeast iso-1-cytochrome c mRNA. Cell. 1981 Jul;25(1):277–284. doi: 10.1016/0092-8674(81)90253-1. [DOI] [PubMed] [Google Scholar]
- Struhl K., Stinchcomb D. T., Scherer S., Davis R. W. High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules. Proc Natl Acad Sci U S A. 1979 Mar;76(3):1035–1039. doi: 10.1073/pnas.76.3.1035. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thill G. P., Kramer R. A., Turner K. J., Bostian K. A. Comparative analysis of the 5'-end regions of two repressible acid phosphatase genes in Saccharomyces cerevisiae. Mol Cell Biol. 1983 Apr;3(4):570–579. doi: 10.1128/mcb.3.4.570. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Toh-E A., Oshima Y. Characterization of a dominant, constitutive mutation, PHOO, for the repressible acid phosphatase synthesis in Saccharomyces cerevisiae. J Bacteriol. 1974 Nov;120(2):608–617. doi: 10.1128/jb.120.2.608-617.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Van Loon A. P., De Groot R. J., De Haan M., Dekker A., Grivell L. A. The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: a protein with an extremely high content of acidic amino acids. EMBO J. 1984 May;3(5):1039–1043. doi: 10.1002/j.1460-2075.1984.tb01924.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zaret K. S., Sherman F. DNA sequence required for efficient transcription termination in yeast. Cell. 1982 Mar;28(3):563–573. doi: 10.1016/0092-8674(82)90211-2. [DOI] [PubMed] [Google Scholar]