1887

Abstract

The nucleotide sequence of the gene () encoding the thermostable α-amylase-pullulanase of was determined. An open reading frame of 4425 bp was present. The deduced polypeptide ( 165600), including a 31 amino acid putative signal sequence, comprised 1475 amino acids, with no cysteine residues. The structural gene was preceded by the consensus promoter sequence TTGACA TATAAT, a putative regulatory sequence and a putative ribosome-binding sequence AAAGGGGG. The codon usage resembled that of genes. The deduced sequence of the mature product showed similarities to various amylolytic enzymes, especially the neopullulanase of , whereas the signal sequence showed similarity to those of the α-amylases of and . Three regions thought to be highly conserved in the primary structure of α-amylases could also be distinguished in the product, two being partly ‘duplicated’ in this α-1,4/α-1,6-active enzyme.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-136-3-447
1990-03-01
2024-04-24
Loading full text...

Full text loading...

/deliver/fulltext/micro/136/3/mic-136-3-447.html?itemId=/content/journal/micro/10.1099/00221287-136-3-447&mimeType=html&fmt=ahah

References

  1. Alff-Steinberger C. 1984; Evidence for a coding pattern on the non-coding strand of the E. coli genome. Nucleic Acids Research 12:2235–2241
    [Google Scholar]
  2. Amemura A., Chakraborty R., Fujita M., Noumi T., Futai M. 1988; Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15*. Journal of Biological Chemistry 263:9271–9275
    [Google Scholar]
  3. Binder F., Huber O., BÖck A. 1986; Cyclodextrin-glycosyltrans-ferase from Klebsiella pneumoniae M5al: cloning, nucleotide sequence and expression. Gene 47:269–277
    [Google Scholar]
  4. Birnboim H. C., Doly J. 1979; A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Research 7:1513–1523
    [Google Scholar]
  5. Coleman R. D., Yang S.-S., Mcalister M. P. 1987; Cloning of the debranching-enzyme gene from Thermoanaerobiumbrockii into Escherichia coli and Bacillus subtilis. Journal of Bacteriology 169:4302–4307
    [Google Scholar]
  6. Crombrugghe B., Busby S., Buc H. 1984; Cyclic AMP receptor protein: role in transcription activation. Science 224:831–838
    [Google Scholar]
  7. Fogarty W. M. 1983; Microbial amylases. In Microbial Enzymes and Biotechnology pp. 1–92 Fogarty W. M. Edited by Barking: Applied Science Publishers;
    [Google Scholar]
  8. Grepinet O., Chebrou M.-C., BÉguin P. 1988; Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum. Journal of Bacteriology 170:4582–4588
    [Google Scholar]
  9. Grosjean H., Fiers W. 1982; Preferential codon usage in procaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Genes 18:199–209
    [Google Scholar]
  10. Hoshiko S., Makabe O., Nojiri C., Katsumata K., Satoh E., Nagaoka K. 1987; Molecular cloning and characterization of the Streptomyces hygroscopicus α-amylase gene. Journal of Bacteriology 169:1029–1036
    [Google Scholar]
  11. Hyun H. H., Zeikus J. G. 1985; Regulation and genetic enhancement of glucoamylase and pullulanase production in Clostridium thermo hydrosulfuricum. Journal of Bacteriology 164:1146–1152
    [Google Scholar]
  12. Imanaka T., Kuriki T. 1989; Pattern of action of Bacillus stearothermophilus neopullulanase on pullulan. Journal of Bacteriology 171:369–374
    [Google Scholar]
  13. Katsuragi N., Takizawa N., Murooka Y. 1987; Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70. Journal of Bacteriology 169:2301–2306
    [Google Scholar]
  14. Kuriki T., Imanaka T. 1989; Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus. Journal of General Microbiology 135:1521–1528
    [Google Scholar]
  15. Kyte J., Doolittle R. F. 1982; A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 157:105–132
    [Google Scholar]
  16. Long C. M., Virolle M.-J., Chang S.-Y., Chang S., Bibb M. J. 1987; α-Amylase gene of Streptomyces limosus: nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate α-Amylases. Journal of Bacteriology 169:5745–5754
    [Google Scholar]
  17. Maniatis T., Fritsch E. F., Sambrook J. 1982 Molecular Cloning: a Laboratory Manual. Cold Spring Harbor, NY:: Cold Spring Harbor Laboratory.;
    [Google Scholar]
  18. Matsuura Y., Kusunoki M., Harada W., Kakudo M. 1984; Structure and possible catalytic residues of Taka-amylase A. Journal of Biochemistry 95:697–702
    [Google Scholar]
  19. Mcconnell D. J., Cantwell B. A., Devine K. M., Forage A. J., Laoide B. M., O’Kane C., Ollington J. F., Sharp P. M. 1986; Genetic engineering of extracellular enzyme systems of bacilli. In Biochemical Engineering IV(Annals of the New York Academy of Sciences 469) pp. 1–17 Lim H. C., Vankatasubramanian K. Edited by New York: New York Academy of Sciences;
    [Google Scholar]
  20. Melasniemi H. 1987; Effect of carbon source on production of thermostableα-amylase, pullulanase andα-glucosidase by Clostridium thermohydrosulfuricum. . Journal of General Microbiology 133:883–890
    [Google Scholar]
  21. Melasniemi H. 1988; Purification and some properties of the extracellularα-amylase-pullulanase produced by Clostridium thermohydrosulfuricum. Biochemical Journal 250:813–818
    [Google Scholar]
  22. Melasniemi H., Paloheimo M. 1989; Cloning and expression of the Clostridium thermohydrosulfuricum α-amylase-pullulanase gene in Escherichia coli. . Journal of General Microbiology 135:1755–1762
    [Google Scholar]
  23. Messing J. 1983; New M13 vectors for cloning. Methods in Enzymology 101:20–78
    [Google Scholar]
  24. Nakajima R., Imanaka T., Aiba S. 1986; Comparison of amino acid sequences of eleven different α-Amylases. Applied Microbiology and Biotechnology 23:355–360
    [Google Scholar]
  25. Norrander J., Kempe T., Messing J. 1983; Construction of improved Ml3 vectors using oligodeoxynucleotide-directed mutagenesis. Gene 26:101–106
    [Google Scholar]
  26. Plant A. R., Clemens R. M., Morgan H. W., Daniel R. M. 1987; Active-site-and substrate-specificity of Thermoanaerobium Tok6-Bl pullulanase. Biochemical Journal 246:537–541
    [Google Scholar]
  27. Rogers J. C. 1985; Two barley α-amylase gene families are regulated differently in aleurone cells. Journal of Biological Chemistry 260:3731–3738
    [Google Scholar]
  28. Rosenberg M., Court D. 1979; Regulatory sequences involved in the promotion and termination of RNA transcription. Annual Review of Genetics 13:319–353
    [Google Scholar]
  29. Sanger F., Nicklen S., Coulson A. R. 1977; DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences of the United States of America 74:5463–5467
    [Google Scholar]
  30. Sata H., Umeda M., Kim C.-H., Taniguchi H., Maruyama Y. 1989; Amylase-pullulanase enzyme produced by B. circulans F-2. Biochimica et BiophysicaActa 991:388–394
    [Google Scholar]
  31. Schwarz W. H., Schimming S., RÜcknagel K. P., Burgsch-Waiger S., Kreil G., Staudenbauer W. L. 1988; Nucleotide sequence of the celC gene encoding endoglucanase C of Clostridium thermocellum. Gene 63:23–30
    [Google Scholar]
  32. Sharon N., Lis H. 1981; Glycoproteins: research booming on long-ignored, ubiquitous compounds. Chemical & Engineering News 30:21–44
    [Google Scholar]
  33. Takano T., Fukuda M., Monma M., Kobayashi S., Kainuma K., Yamane K. 1986; Molecular cloning, DNA nucleotide sequencing, and expression in Bacillus subtilis cells of the Bacillus macerans cyclodextrin glucanotransferase gene. Journal of Bacteriology 166:1118–1122
    [Google Scholar]
  34. Takasaki Y. 1987; Pullulanase-amylase complex enzyme from Bacillus subtilis. Agricultural and Biological Chemistry 51:9–16
    [Google Scholar]
  35. Wiegel J., Ljungdahl L. G., Rawson J. R. 1979; Isolation from soil and properties of the extreme thermophile Clostridium thermohydrosulfuricum. Journal of Bacteriology 139:800–810
    [Google Scholar]
  36. Yanisch-Perron C., Vieira J., 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]
  37. Yuuki T., Nomura T., Tezuka H., Tsuboi A., Yamagata H., Tsukagoshi N., Udaka S. 1985; Complete nucleotide sequence of a gene coding for heat-and pH-stable α-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying α-Amylases deduced from the DNA sequences. Journal of Biochemistry 98:1147–1156
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-136-3-447
Loading
/content/journal/micro/10.1099/00221287-136-3-447
Loading

Data & Media loading...

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