1887

Abstract

A partial 3Al digest of genomic DNA from was cloned in a shuttle vector, and the recombinant plasmids were used to transform CGSC 6212, which carries a mutation in the gene for aspartate semialdehyde dehydrogenase (Asd). One of 39000 transformants tested grew on LB medium lacking diaminopimelate. A 17 kb plasmid (pJV21) isolated from this strain conferred prototrophy when used to transform CGSC 6212. The gene responsible was located on a 2.2 kb DNA fragment by subcloning. Nucleotide sequencing and codon preference analysis of the subcloned insert and of the 3.3 kb insert in the Asd -complementing plasmid pJV36 located three complete and two incomplete open reading frames (ORFs). One of these (ORF3), encoding a polypeptide of 338 amino acids 35484), was identified as the gene for Asd by comparing its sequence with database sequences of from other bacteria. The inability of pJV30, in which a segment of ORF3 had been deleted, to transform CGSC 6212 to prototrophy supported this assignment. Southern hybridization indicated that the sequenced region of the cloned DNA fragment represented a continuous segment of the chromosome. The deduced amino acid sequences of the ORFs adjacent to showed no similarity to sequences for aspartate kinase (Ask); also, transformation with plasmids containing and adjacent regions from the chromosome did not complement the mutant CGSC 5074. It is concluded that and in are not present in an operon, and thus are organized differently from these genes in the Gram-positive bacteria previously examined.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-142-4-791
1996-04-01
2021-10-23
Loading full text...

Full text loading...

/deliver/fulltext/micro/142/4/mic-142-4-791.html?itemId=/content/journal/micro/10.1099/00221287-142-4-791&mimeType=html&fmt=ahah

References

  1. Adhya S., Gottesman M. Control of transcription termination. Amu Rep Biochem 1978; 47:967–996
    [Google Scholar]
  2. Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J. Basic local alignment search tool. J Mol Biol 1990; 215:403–410
    [Google Scholar]
  3. Baltz R.H. Gene expression using streptomycetes. Curr Opin Biotechnol 1990; 1:12–20
    [Google Scholar]
  4. Bender E., Koller K.-P., Engels J.W. Secretory synthesis of human interleukin-2 by Streptomyces lividans. Gene 1990; 86:227–232
    [Google Scholar]
  5. Biellmann J.-F., Eid P., Hirth C., Jornavall H. Aspartate-β-semialdehyde dehydrogenase from Escherichia coli. Eur J Biochem 1980; 104:59–64
    [Google Scholar]
  6. Butler M.J., Aphale J.S., Binnie C., Di Zonno M.A., Krygsman P., Soltes G., A., Walczyk E., Malek L.T. A gene encoding an aminopeptidase N from 3 lividans 66. Gene 1994; 141:115–119
    [Google Scholar]
  7. Cardineau G.A., Curtiss R. Nucleotide sequence of the asd gene of Streptococcus mutans. J Biol Chem 1987; 262:3344–3553
    [Google Scholar]
  8. Chen N.-Y., Jiang S.-Q., Klein D.A., Paulus H. Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J Biol Chem 1993; 268:9448–9465
    [Google Scholar]
  9. Cirillo J.D., Barletta R.G., Bloom B.R., Jacobs W.R. Jr A novel transposon for mycobacteria: isolation and characterization of IS 1096. J Bacteriol 1991; 173:7772–7780
    [Google Scholar]
  10. Cirillo J.D., Weisbrod T.R., Pascopella L., Bloom B.R., Jacobs W.R. Jr Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria. Mol Microbiol 1994; 11:629–639
    [Google Scholar]
  11. Cohen G.N., Stanier R.Y., Le Bras G. Regulation of the biosynthesis of amino acids of the aspartate family in coliform bacteria and pseudomonads. J Bacteriol 1969; 99:791–801
    [Google Scholar]
  12. Cremer J., Treptow C., Eggeling L., Sahm H. Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum. J Gen Microbiol 1988; 134:3221–3229
    [Google Scholar]
  13. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 1984; 12:387–395
    [Google Scholar]
  14. Feinberg A.P., Vogelstein B. A technique for radiolabeling restriction endonuclease fragments to high specific activity. Anal Biochem 1983; 132:6–13
    [Google Scholar]
  15. Higgins D.G., Sharp P.M. Clustal: a package for performing multiple sequence alignments on a microcomputer. Gene 1988; 73:237–244
    [Google Scholar]
  16. Hopwood D.A., Bibb M.J., Chater K.F., Kieser T., Bruton C.J., Kieser H.M., Lydiate D.J., Smith C.P., Ward J.M., Schrempf H. Genetic Manipulation of Streptomyces: a Laboratory Manual 1985 Norwich: John Innes Foundation;
    [Google Scholar]
  17. Kalinowski J., Bachmann B., Thierbach G., Puhler A. Aspartokinase genes lysCa. and lysCfi overlap and are adjacent to the aspartate /i-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum. Mol b Gen Genet 1990; 224:317–324
    [Google Scholar]
  18. Kanazawa K., Tsuchiya K., Araki T. A new antituberculosis amino acid (5-hydroxy-4-oxo-L-norvaline. Am Ren Resp Dis 1960; 81:924–1
    [Google Scholar]
  19. Larson J.L., Hershberger C.L. The minimum replicon of a streptomycete plasmid produces an ultrahigh level of plasmid DNA. Plasmid 1986; 15:199–209
    [Google Scholar]
  20. Le Y. Biosynthesis of 5-hydroxy-4-oxonorvaline and aspartate family amino acids in Streptomyces akiyoshiensis 1994 PhD thesis, Dalhousie University, Halifax, Canada;
    [Google Scholar]
  21. Lee S.-Y., Rasheed S. A simple procedure for maximum yield of high quality plasmid DNA. BioTechniques 1990; 9:676–679
    [Google Scholar]
  22. Lonetto M., Brown K.L., Rudd K., Buttner M.J. Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase sigma factors involved in the regulation of extracytoplasmic functions. Proc Natl AcadSci USA 1994; 91:7573–7577
    [Google Scholar]
  23. Madduri K., Stuttard C., Vining L.C. Lysine catabolism in Streptomyces spp. is primarily through cadaverine: β-lactam producers also make a-aminoadipate. J Bacteriol 1989; 171:299–302
    [Google Scholar]
  24. Marck C. ‘ DNA Strider’: a ‘C’ program for the fast analysis of DNA and protein sequences on the Apple Macintosh family of computers. Nucleic Acids Res 1988; 16:1829–1836
    [Google Scholar]
  25. Mead D.A., Kemper B. Chimeric single-strand DNA phage-plasmid cloning vectors. In Vectors 1988 Edited by Rodriguez R.L., Denhardt D.T. Toronto: Butterworths; pp 85–102
    [Google Scholar]
  26. Mendelovitz S., Aharonowitz Y. Regulation of cephamycin C synthesis, aspartokinase, dihydrodipicolinic acid synthetase and homoserine dehydrogenase by aspartic acid family amino acids in Streptomyces clavuligerus. Antimicrob Agents Chemother 1982; 21:74–84
    [Google Scholar]
  27. Nakayama K., Kelly S., Curtiss R. Construction of an Asd+ expression vector: stable maintenance and high level expression of cloned genes in a Salmonella vaccine strain. Bio/Technology 1988; 6:693–697
    [Google Scholar]
  28. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: a Laboratory Manual, 2nd edn 1989 Cold Spring Harbor, NY: Cold Spring Harbour Laboratory;
    [Google Scholar]
  29. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977; 74:5463–5467
    [Google Scholar]
  30. Seno E., T. & Baltz R.H. Structural organization of antibiotic biosynthesis and resistance genes in actinomyces. In Regulation of Secondary Metabolites in Actinomycetes 1989 Edited by Shapiro S. Boca Raton, FL: CRC Press; pp 1–48
    [Google Scholar]
  31. Shiio I., Miyajima R. Concerted inhibition and its reversal by end-products of aspartate kinase in Brevibacterium flavum. J Biochem 1969; 65:849–859
    [Google Scholar]
  32. Strohl W.R. Compilation and analysis of DNA sequences associated with apparent streptomycete promoters. Nucleic Acids Rfr 1992; 20:961–974
    [Google Scholar]
  33. Stuttard C. Temperate phages of Streptomyces venezuelae: lysogeny and host specificity shown by phages SV1 and SV2. J Gen Microbiol 1982; 128:115–121
    [Google Scholar]
  34. Stuttard C. Transduction and genome structure in Streptomyces. Dev Ind Microbiol 1988; 29:69–76
    [Google Scholar]
  35. Takaguchi S., Kumagai I., Nakayama J., Suzuki A., Miura K. Efficient extracellular expression of a foreign protein in Streptomyces using secretory protease inhibitor (SSI) gene fusion. Bio/Technology 1989; 7:1063–1066
    [Google Scholar]
  36. Theze J., Margarita D., Cohen G.N., Borne F., Patte J.C. Mapping of the structural genes of three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K12. J Bacteriol 1974; 117:133–143
    [Google Scholar]
  37. Thomas D., Surdin-Kerjan Y. Structure of the HOM2 gene of Saccharomyces cerevisiae and regulation of its expression. Mol & Gen Genet 1989; 217:149–154
    [Google Scholar]
  38. Tinoco I. Jr, Borer P.N., Dengler B., Levine M.D., Uhlenbeck O.C., Crothers D.M., Gralla J. Improved estimation of secondary structure in ribonucleic acids. Nature New Biol 1973; 246:40–41
    [Google Scholar]
  39. Vining L.C., Shapiro S., Madduri K., Stuttard C. Biosynthesis and control of /Mactam antibiotics: the early steps in the ‘classical’ tripeptide pathway. Biotechnol Adv 1990; 8:159–183
    [Google Scholar]
  40. White R.L., De Marco A.C., Smith K.C. Biosynthesis of the unusual amino acid 5-hydroxy-4-oxonorvaline. J Am Chem Soc 1988; 110:8228–8229
    [Google Scholar]
  41. Whitney J.G., Brannon D.R., Mabe J.A., Wicker K.J. Incorporation of labeled precursors into A16886B, a novel /Mactam antibiotic produced by Streptomyces clavuligerus. Antimicrob Agents Chemother 1972; 1:247–251
    [Google Scholar]
  42. Wright F., Bibb M.J. Codon usage in the G + C rich Streptomyces genome. Gene 1992; 113:55–65
    [Google Scholar]
  43. Yamaguchi M., Yamaki H., Shinoda T., Yoshitaka T., Suzuki H., Nishimura T., Yamaguchi H. The mode of antifungal action of (Y)-2-amino-4-oxo-5-hydroxypentanoic acid RI-331. J Antibiot 1990; 43:411–416
    [Google Scholar]
  44. Yeh P., Sicard A.M., Sinskey A.J. General organization of the genes specifically involved in the diaminopimelate-lysine biosynthetic pathway of Corynebacterium glutamicum. Mol & Gen Genet 1988; 212:105–111
    [Google Scholar]
  45. Zhang J.-J., Hu F.-M., Chen N.-Y., Paulus H. Comparison of the three aspartokinase isoenzymes in Bacillus subtilis Marburg and 168. J Bacteriol 1990; 172:701–708
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-142-4-791
Loading
/content/journal/micro/10.1099/00221287-142-4-791
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error