Molecular and General Genetics MGG

, Volume 191, Issue 3, pp 339–346 | Cite as

An insertion mutation associated with constitutive expression of repressible acid phosphatase in Saccharomyces cerevisiae

  • Akio Toh-e
  • Yoshinobu Kaneko
  • Jirô Akimaru
  • Yasuji Oshima


The PHO83 mutation in Saccharomyces cerevisiae, which had been detected on the basis of constitutive production of repressible acid phosphatase and mapped at the end of the PHO5 locus, was analysed by Southern hybridization with cloned DNA fragments of the PHO5 gene as probe. It was shown that this mutant has a DNA insertion of about 6 kilobase pairs, probably in the 5′-noncoding region of the PHO5 gene. Production of repressible acid phosphatase by the PHO83 mutant is partially independent of the function of the PHO2 and PHO4 genes, the positive regulatory genes whose functions are indispensable for PHO5 expression. PHO83 mutants are constitutive in a or α cells, either haploid or diploid, but not in non-mating cells, MATa/MATα or a certain sterile mutation. These observations strongly suggest that the PHO83 mutation is caused by insertion of a Ty element in the 5′-noncoding region of the PHO5 gene.


Regulatory Gene Saccharomyces Cerevisiae Saccharomyces Acid Phosphatase Constitutive Expression 
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  1. Andersen N, Thill GP, Kramer RA (1983) RNA and homology mapping of two DNA fragments with repressible acid phosphatase genes from Saccharomyces cerevisiae. Mol Cell Biol 3:562–569Google Scholar
  2. Bostian KA, Lemire JM, Cannon LE, Halvorson HO (1980) In vitro synthesis of repressible yeast acid phosphatase: Identification of multiple mRNAs and products. Proc Natl Acad Sci USA 77:4504–4508Google Scholar
  3. Clewell DB, Helinski DR (1969) Supercoiled circular DNA-protein complex in Escherichia coli: purification and induced conversion to an open circular DNA. Proc Natl Acad Sci USA 62:1159–1166Google Scholar
  4. Deschamps J, Wiame JM (1979) Mating-type effect on cis mutations leading to constitutivity of ornithine transaminase in diploid cells of Saccharomyces cerevisiae. Genetics 92:749–758Google Scholar
  5. Dubois E, Hiernaux D, Grenson M, Wiame JM (1978) Specific induction of catabolism and its relation to repression of biosynthesis in arginine metabolism of Saccharomyces cerevisiae. J Mol Biol 122:383–406Google Scholar
  6. Errede B, Cardillo TS, Sherman F, Dubois E, Deschamps J, Wiame JM (1980) Mating signals control expression of mutations resulting from insertion of a transposable repetitive element adjacent to diverse yeast genes. Cell 22:427–436Google Scholar
  7. Hemmings BA, Zubenko GS, Hasilik A, Jones EW (1981) Mutant defective in processing of an enzyme located in the lysosomelike vacuole of Saccharomyces cerevisiae. Proc Natl Acad Sci USA 78:435–439Google Scholar
  8. Hereford L, Fahrner K, Woolford Jr. J, Rosbash M, Kaback DB (1979) Isolation of yeast histone genes H2A and H2B. Cell 18:1261–1271Google Scholar
  9. Jeffreys AJ, Flavell RA (1977) A physical map of the DNA regions flanking the rabbit β-globin gene. Cell 12:429–439Google Scholar
  10. Kaneko Y, Toh-e A, Oshima Y (1982) Identification of the genetic locus for the structural gene and a new regulatory gene for the synthesis of repressible alkaline phosphatase in Saccharomyces cerevisiae. Mol Cell Biol 2:127–137Google Scholar
  11. Kramer R, Andersen N (1980) Isoration of yeast genes with mRNA levels controlled by phosphate concentration. Proc Natl Acad Sci USA 77:6541–6545Google Scholar
  12. Lemoine Y, Dubois E, Wiame JM (1978) The regulation of urea amidolyase of Saccharomyces cerevisiae. Mating type influence on a constitutivity mutation acting in cis. Mol Gen Genet 166:251–258Google Scholar
  13. Matsumoto K, Adachi Y, Toh-e A, Oshima Y (1980) Function of positive regulatory gene gal4 in the synthesis of galactose pathway enzymes in Saccharomyces cerevisiae: evidence that the Gal81 region codes for part of the gal4 protein. J Bacteriol 141:508–527Google Scholar
  14. Meyhack B, Bajwa W, Rudolph H, Hinnen A (1982) 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 1:675–680Google Scholar
  15. Miller JH (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, New YorkGoogle Scholar
  16. Rigby PWJ, Dieckmann M, Rhgodes C, Berg P (1977) Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol 113:237–251Google Scholar
  17. Roeder GS, Fink GR (1980) DNA rearrangements associated with a transposable element in yeast. Cell 21:239–249Google Scholar
  18. Rogers DT, Lemire JM, Bostian KA (1982) Acid phosphatase polypeptides in Saccharomyces cerevisiae are encoded by a differentially regulated multigene family. Proc Natl Acad Sci USA 79:2157–2161Google Scholar
  19. Rothstein RJ, Sherman F (1980) Dependence on mating type for the overproduction of iso-2-cytochrome c in the yeast mutant CYC7-H2. Genetics 94:891–898Google Scholar
  20. Rubin CM (1974) Three forms of the 5.8 S ribosomal RNA species in Saccharomyces cerevisiae. Eur J Biochem 41:197–202Google Scholar
  21. Schurr A, Yagil E (1971) Regulation and characterization of acid and alkaline phosphatase in yeast. J Gen Microbiol 65:291–303Google Scholar
  22. Southern EM (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol 98:503–517Google Scholar
  23. Szybalski EH, Szybalski W (1979) A comprehensive molecular map of bacteriophage lambda. Gene 7:217–270Google Scholar
  24. Tanaka T, Weisblum B (1975) Construction of a colicin E1-R factor composite plasmid in vitro: means for amplification of deoxyribonucleic acid. J Bacteriol 121:354–362Google Scholar
  25. Thill GP, Kramer RA, Turner KJ, Bostian KA (1983) Comparative analysis of the 5′-end regions of two repressible acid phosphatase genes in Saccharomyces cerevisiae. Mol Cell Biol 3:570–579Google Scholar
  26. Toh-e A, Inouye S, Oshima Y (1981) Structure and function of the PHO82-pho4 locus controlling the synthesis of repressible acid phosphatase of Saccharomyces cerevisiae. J Bacteriol 145:221–232Google Scholar
  27. Toh-e A, Kakimoto S, Oshima Y (1975a) Two new genes controlling the constitutive acid phosphatase synthesis in Saccharomyces cerevisiae. Mol Gen Genet 141:81–83Google Scholar
  28. Toh-e A, Kakimoto S, Oshima Y (1975b) Genes coding for the structure of the acid phosphatases in Saccharomyces cerevisiae. Mol Gen Genet 143:65–70Google Scholar
  29. Toh-e A, Nakamura H, Oshima Y (1976) A gene controlling the synthesis of non-specific alkaline phosphatase in Saccharomyces cerevisiae. Biochim Biophys Acta 428:182–192Google Scholar
  30. Toh-e A, Oshima Y (1974) Characterization of a dominant, constitutive mutation, PHOO, for the repressible acid phosphatase synthesis in Saccharomyces cerevisiae. J Bacteriol 120:608–617Google Scholar
  31. Toh-e A, Oshima Y (1975) Regulation of acid phosphatase synthesis in Saccharomyces cerevisiae. In: Hasegawa T (ed) Proceedings of the First Intersectional Congress of the International Association of Microbiological Societies, vol 1. Science Council of Japan, Tokyo, pp 396–399Google Scholar
  32. Toh-e A, Ueda Y, Kakimoto S, Oshima Y (1973) Isolation and characterization of acid phosphatase mutants in Saccharomyces cerevisiae. J Bacteriol 113:727–738Google Scholar
  33. Weiss B (1971) DNA ligase from Escherichia coli infected with bacteriophage T4. Methods Enzymol 21:319–326Google Scholar
  34. Williamson VM, Young ET, Ciriacy M (1981) Transposable elements associated with constitutive expression of yeast alcohol dehydrogenase II. Cell 23:605–614Google Scholar

Copyright information

© Springer-Verlag 1983

Authors and Affiliations

  • Akio Toh-e
    • 1
  • Yoshinobu Kaneko
    • 2
  • Jirô Akimaru
    • 2
  • Yasuji Oshima
    • 2
  1. 1.Department of Fermentation TechnologyHiroshima UniversityHigashihiroshima-shi, Hiroshima
  2. 2.Department of Fermentation TechnologyOsaka UniversitySuita-shi, OsakaJapan

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