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. 1979 Feb;137(2):802–810. doi: 10.1128/jb.137.2.802-810.1979

Promoter-like mutants with increased expression of the Escherichia coli uridine phosphorylase structural gene.

A S Mironov, V V Sukhodolets
PMCID: PMC218360  PMID: 370101

Abstract

From an Escherichia coli K-12 strain lacking adenylate cyclase (cya) and cyclic AMP receptor protein (crp), two mutants were isolated that synthesize uridine phosphorylase constitutively. The mutations differ from one another and also from a wild type in the maximum rate of uridine phosphorylase synthesis. They have constitutive expression of the uridine phosphorylase gene (udp) in the presence of repressor protein coded by the cytR regulatory gene and decrease the sensitivity of the udp gene simultaneously with catabolite repression. Both mutations cause a high level of udp expression whether they are in a cya crp or in a cya+ crp+ background. Another mutation (udpP1) isolated previously alters the response of udp gene to the ctyR repressor and produces a higher constitutive level of uridine phosphorylase in a cytR+ than in a cytR background when bacteria are grown in glucose. The synthesis of uridine phosphorylase in this mutant is dependent on an intact cyclic AMP-cyclic AMP receptor protein complex. All mutations studied are cis-acting and extremely closely linked to the udp structural gene, and appear to affect the uridine phosphorylase promoter-operator region. The data obtained are in accordance with a suggestion that the cytR repressor protein normally asserts its function by preventing the positive action of cyclic AMP-cyclic AMP receptor protein complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arditti R., Grodzicker T., Beckwith J. Cyclic adenosine monophosphate-independent mutants of the lactose operon of Escherichia coli. J Bacteriol. 1973 May;114(2):652–655. doi: 10.1128/jb.114.2.652-655.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bastarrachea F., Willetts N. S. The elimination by acridine orange of F30 from recombination-deficient strains of Escherichia coli K12. Genetics. 1968 Jun;59(2):153–166. doi: 10.1093/genetics/59.2.153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Beacham I. R., Pritchard R. H. The role of nucleoside phosphorylases in the degradation of deoxyribonucleosides by thymine-requiring mutants of E. coli. Mol Gen Genet. 1971;110(4):289–298. doi: 10.1007/BF00438271. [DOI] [PubMed] [Google Scholar]
  4. Beckwith J., Grodzicker T., Arditti R. Evidence for two sites in the lac promoter region. J Mol Biol. 1972 Aug 14;69(1):155–160. doi: 10.1016/0022-2836(72)90031-9. [DOI] [PubMed] [Google Scholar]
  5. Bilezikian J. P., Kaempfer R. O., Magasanik B. Mechanism of tryptophanase induction in Escherichia coli. J Mol Biol. 1967 Aug 14;27(3):495–506. doi: 10.1016/0022-2836(67)90054-x. [DOI] [PubMed] [Google Scholar]
  6. Bloom F. R., McFall E., Young M. C., Carothers A. M. Positive control in the D-serine deaminase system of Escherichia coli K-12. J Bacteriol. 1975 Mar;121(3):1092–1101. doi: 10.1128/jb.121.3.1092-1101.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Buxton R. S. Genetic analysis of thymidine-resistant and low-thymine-requiring mutants of Escherichia coli K-12 induced by bacteriophage Mu-1. J Bacteriol. 1975 Feb;121(2):475–484. doi: 10.1128/jb.121.2.475-484.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hammer-Jespersen K., Munch-Ptersen A. Multiple regulation of nucleoside catabolizing enzymes: regulation of the deo operon by the cytR and deoR gene products. Mol Gen Genet. 1975;137(4):327–335. doi: 10.1007/BF00703258. [DOI] [PubMed] [Google Scholar]
  9. Hammer-Jespersen K., Nygaard P. Multiple regulation of nucleoside catabolizing enzymes in Escherichia coli: effects of 3:5' cyclic AMP and CRP protein. Mol Gen Genet. 1976 Oct 18;148(1):49–55. doi: 10.1007/BF00268545. [DOI] [PubMed] [Google Scholar]
  10. Hopkins J. D. A new class of promoter mutations in the lactose operon of Escherichia coli. J Mol Biol. 1974 Aug 25;87(4):715–724. doi: 10.1016/0022-2836(74)90080-1. [DOI] [PubMed] [Google Scholar]
  11. Jackson E. N., Yanofsky C. Duplication-translocations of tryptophan operon genes in Escherichia coli. J Bacteriol. 1973 Oct;116(1):33–40. doi: 10.1128/jb.116.1.33-40.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Leer J. C., Hammer-Jespersen K., Schwartz M. Uridine phosphorylase from Escherichia coli. Physical and chemical characterization. Eur J Biochem. 1977 May 2;75(1):217–224. doi: 10.1111/j.1432-1033.1977.tb11520.x. [DOI] [PubMed] [Google Scholar]
  15. McFall E. Role of adenosine 3',5'-cyclic monophosphate and its specific binding protein in the regulation of D-serine deaminase synthesis. J Bacteriol. 1973 Feb;113(2):781–785. doi: 10.1128/jb.113.2.781-785.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mironov A. S., Sukhodolets V. V., Alkhimova R. A. Vliianie mutatsii po adenilattsiklaze (cya) i belku-retseptoru tsiklicheskogo adenozinmonofosfata (cgp) na vyrazhenie genov katabolizma nukleozidov u Escherichia coli. Genetika. 1978;14(1):103–110. [PubMed] [Google Scholar]
  17. Munch-Petersen A., Nygaard P., Hammer-Jespersen K., Fiil N. Mutants constitutive for nucleoside-catabolizing enzymes in Escherichia coli K12. Isolation, charactrization and mapping. Eur J Biochem. 1972 May 23;27(2):208–215. doi: 10.1111/j.1432-1033.1972.tb01828.x. [DOI] [PubMed] [Google Scholar]
  18. Musso R., Di Lauro R., Rosenberg M., de Crombrugghe B. Nucleotide sequence of the operator-promoter region of the galactose operon of Escherichia coli. Proc Natl Acad Sci U S A. 1977 Jan;74(1):106–110. doi: 10.1073/pnas.74.1.106. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. PAEGE L. M., SCHLENK F. Bacterial uracil riboside phosphorylase. Arch Biochem Biophys. 1952 Sep;40(1):42–49. doi: 10.1016/0003-9861(52)90071-4. [DOI] [PubMed] [Google Scholar]
  20. Pritchard R. H., Ahmad S. I. Fluorouracil and the isolation of mutants lacking uridine phosphorylase in Escherichia coli: location of the gene. Mol Gen Genet. 1971;111(1):84–88. doi: 10.1007/BF00286557. [DOI] [PubMed] [Google Scholar]
  21. RAZZELL W. E., KHORANA H. G. Purification and properties of a pyrimidine deoxyriboside phosphorylase from Escherichia coli. Biochim Biophys Acta. 1958 Jun;28(3):562–566. doi: 10.1016/0006-3002(58)90519-5. [DOI] [PubMed] [Google Scholar]
  22. Yudkin M. D. Unstable mutations that relieve catabolite repression of tryptophanase synthesis by Escherichia coli. J Bacteriol. 1977 Apr;130(1):57–61. doi: 10.1128/jb.130.1.57-61.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]

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