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Volume 141, Issue 5

An operon encoding aspartokinase and purine phosphoribosyltransferase in Free

Abstract

SUMMARY

The nucleotide sequence of a 1:1 kb l-III fragment downstream of the malate dehydrogenase () gene of revealed the presence of an ORF and an incomplete ORF lacking its NH-terminal portion, in the opposite orientation to that of the gene. These two genes overlapped with each other, sharing two base pairs, suggesting that these genes are co-transcribed in a single mRNA. One ORF (termed ) encoded a protein of 154 amino acids showing significant amino acid sequence similarity to purine phosphoribosyltransferases, such as xanthine-guanine phosphoribosyltransferase of and human hypoxanthine phosphoribosyltransferase. Cloning and sequencing of the upstream region of the gene, together with sequence comparison of the gene product encoded by the region upstream of , suggested that the upstream ORF encoded two in-frame overlapping aspartokinase genes, , encoding the β-subunit of 405 amino acids, and , encoding the β-subunit of 161 amino acids, which was part of the 3′ portion of . Consistent with the sequence data, the and the genes conferred the heat-stable enzyme activities of aspartokinase and phosphoribosyltransferase, respectively, on . Preliminary characterization of these enzymes produced in is described.

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Keyword(s): aspartokinase , end-product inhibition , purine phosphoribosyltransferase , thermostable enzyme and Thermus flavus
© Society for General Microbiology 1995
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1995-05-01
2024-04-19
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References

  1. Bradford M.M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.. Anal Biochem 72:248–254
     [Google Scholar]
  2. Buck D., Spencer M.E., Guest J.R. 1985; Primary sequence of the succinyl-CoA synthetase from Escherichia coli. . Biochemistry 24:6245–6252
     [Google Scholar]
  3. Cassan M., Parsot C., Cohen G.N., Patte J.-C. 1986; Nucleotide sequence of lysC gene encoding the lysine-sensitive aspartokinase III of Escherichia coli K12.. J Biol Chem 261:1053–1057
     [Google Scholar]
  4. Chen N.-Y., Paulus H. 1988; Mechanism of expression of the overlapping genes of Bacillus subtilis aspartokinase II.. J Biol Chem 263:9526–9532
     [Google Scholar]
  5. Chen N.-Y., Hu F.-M., Paulus H. 1987; Nucleotide sequence of the overlapping genes for the subunits of Bacillus subtilis aspartokinase II and their control region.. J Biol Chem 262:8787–8798
     [Google Scholar]
  6. Chen N.-Y., Zhang J., Paulus H. 1989; Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli. . J Gen Microbiol 135:2931–2940
     [Google Scholar]
  7. Cirillo J.D., Weisbrod T.R., Pascopella L., Bloom B.R., Jacobs W.R. Jr 1994; Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria.. Mol Microbiol 11:629–639
     [Google Scholar]
  8. Cohen G.N. 1985; Aspartate kinases I, II, and III from Escherichia coli. . Methods Envymol 113:596–599
     [Google Scholar]
  9. Darlison M.G., Guest J.R. 1984; Nucleotide sequence of the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli. . Biochem J 223:507–517
     [Google Scholar]
  10. Darlison M.G., Spencer M.E., Guest J.R. 1984; Nucleotide sequence of the sue A gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12.. Eur J Biochem 141:351–359
     [Google Scholar]
  11. Duchange N., Zakin M.M., Ferrara P., Saint Girons I., Park I., Tran S.V., Py M.-C., Cohen G.N. 1983; Structure of the metJBEF cluster in Escherichia coli K12.. J Biol Chem 258:14868–14871
     [Google Scholar]
  12. Grunstein M., Hogness D.S. 1975; Colony hybridization: a method for isolation of cloned DNAs that contain a specific gene.. Proc Natl Acad Sci USA 72:3961–3965
     [Google Scholar]
  13. Heard J.T. Jr Butler M.A., Baptist J.N., Matney T.S. 1975; Chromosomal location of mutations affecting the electrophoretic mobility of malate dehydrogenase in Escherichia coli K-12.. J Bacteriol 122:329–331
     [Google Scholar]
  14. Iijima S., Uozumi T., Beppu T. 1986; Molecular cloning of Thermus flavus malate dehydrogenase gene.. Agric Biol Chem 50:589–592
     [Google Scholar]
  15. Jolly D.J., Okayama H., Berg P., Esty A.C., Filpula D., Bohlen P., Johnson G.G., Shively J.E., Hunkapillar T., Friedmann T. 1983; Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyltransferase.. Proc Natl Acad Sci USA 80:477–481
     [Google Scholar]
  16. Kalinowski J., Bachmann B., Thierbach G., PUhler A. 1990; Aspartokinase genes lysCα and lysCβ overlap and are adjacent to the aspartate β-semialdehyde dehydrogenase gene asd in Corjnebacterium glutamicum. . Mol & Gen Genet 224:317–324
     [Google Scholar]
  17. Kalinowski J., Cremer J., Bachmann B., Eggeling L., Sahm H. 1991; Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum. . Mol Microbiol 5:1197–1204
     [Google Scholar]
  18. Katinka M., Cossart P., Sibilli L., Saint Girons I., Chalvignac M.A., Le Bras, Cohen G.N., Yaniv M. 1980; Nucleotide sequence of the thrA gene of Escherichia coli. . Proc Natl Acad Sci USA 77:5730–5733
     [Google Scholar]
  19. Lu Y., Shevtchenko T.N., Pauius H. 1992; Fine-structure mapping of ar-acting control sites in the lysC operon of Bacillus subtilis. . FEMS Microbiol Lett 92:23–28
     [Google Scholar]
  20. Messing J. 1983; New Ml3 vectors for cloning.. Methods Ensgymol 101:20–78
     [Google Scholar]
  21. Moir D., Pauius H. 1977; Properties and subunit structure of aspartokinase II from Bacillus subtilis VB217.. J Biol Chem 252:4648–4654
     [Google Scholar]
  22. Nishiyama M., Matsubara N., Yamamoto K., Iijima S., Uozumi T., Beppu T. 1986; Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity.. J Biol Chem 261:14178–14183
     [Google Scholar]
  23. Nishiyama M., Horinouchi S., Beppu T. 1991; Characterization of an operon encoding succinyl-CoA synthetase and malate dehydrogenase from Thermus flavus AT-62 and its expression in Escherichia coli. . Mol & Gen Genet 226:1–9
     [Google Scholar]
  24. Pratt D., Subramani S. 1983; Nucleotide sequence of the Escherichia coli xanthine-guanine phosphoribosyltransferase gene.. Nucleic Acids Res 11:8817–8823
     [Google Scholar]
  25. Saito H., Miura K. 1963; Preparation of transforming deoxyribonucleic acid by phenol treatment.. Biochim Biophys Acta 72:619–629
     [Google Scholar]
  26. Sanger F., Nicklen S., Coulson A.R. 1977; DNA sequencing with chain-terminating inhibitors.. Proc Natl Acad Sci USA 74:5463–5467
     [Google Scholar]
  27. Southerland P., McAlister-Henn L. 1985; Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase.. J Bacteriol 163:1074–1079
     [Google Scholar]
  28. Southern E.M. 1975; Detection of specific sequences among DNA fragments separated by agarose gel electrophoresis.. J Mol Biol 98:503–517
     [Google Scholar]
  29. Spencer M.E., Darlison M.G., Stephens P.E., Duckenfield I.K., Guest J.R. 1984; Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase.. Eur J Biochem 141:361–374
     [Google Scholar]
  30. Theze J., Saint Girons I. 1974; Threonine locus of Escherichia coli K-12: genetic structure and evidence for an operon.. J Bacteriol 118:990–998
     [Google Scholar]
  31. Tosaka O., Enei H., Hirose Y. 1983; The production of l-lysine by fermentation.. Trends Biotechnol 1:70–76
     [Google Scholar]
  32. Wood D., Darlison M.G., Wild R.J., Guest J.R. 1984; Nucleotide sequence of the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. . Biochem J 222:519–534
     [Google Scholar]
  33. Yanisch-Perron G, Messing J. 1985; Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mpl8 and pUC19 vectors.. Gene 33:103–119
     [Google Scholar]
  34. Zakin M.M., Duchange N., Ferrara P., Cohen G.N. 1983; Nucleotide sequence of the metL gene of Escherichia coli. . J Biol Chem 258:3028–3031
     [Google Scholar]
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An operon encoding aspartokinase and purine phosphoribosyltransferase in Thermus flavus
Microbiology 141, 1211 (1995); https://doi.org/10.1099/13500872-141-5-1211
/content/journal/micro/10.1099/13500872-141-5-1211
/content/journal/micro/10.1099/13500872-141-5-1211
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