Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1988 Mar;170(3):1034–1040. doi: 10.1128/jb.170.3.1034-1040.1988

Evidence for movement of the alpha-amylase gene into two phylogenetically distant Bacillus stearothermophilus strains.

H Satoh 1, H Nishida 1, K Isono 1
PMCID: PMC210870  PMID: 3257753

Abstract

The gene for an alpha-amylase cloned from strain DY-5 of Bacillus stearothermophilus was used to examine to what extent the corresponding genes are structurally similar in other B. stearothermophilus strains. The structure of the gene itself was almost identical in DY-5 and a group of strains represented by strain 799. The gene was not detected at all in strain DSM2334, which was phenotypically amylase deficient. Comparison of the structure of 5S rRNA and electrophoretic pattern of the ribosomal proteins indicates that strains DY-5 and DSM2334 are closely related to each other, whereas strain 799 is phylogenetically very distant from the two. We estimate that strain 799 separated from DY-5 and DSM2334 some 420 million years ago. Nucleotide sequencing of the region containing the amylase gene from strains DY-5 and 799 revealed the presence of a 3.4-kilobase stretch that was highly similar in the two strains. Furthermore, comparison of the restriction map surrounding the amylase gene of DY-5 with that of a corresponding region in DSM2334 indicated that the former strain contained an extra segment 5.5 kilobases in length, which included the 3.4-kilobase stretch mentioned above. This segment was missing in DSM2334. It thus appears that the alpha-amylase gene was brought into strains DY-5 and 799 from outside despite a large phylogenetic distance.

Full text

PDF
1034

Images in this article

Selected References

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

  1. Brownlee G. G., Sanger F. Nucleotide sequences from the low molecular weight ribosomal RNA of Escherichia coli. J Mol Biol. 1967 Feb 14;23(3):337–353. doi: 10.1016/s0022-2836(67)80109-8. [DOI] [PubMed] [Google Scholar]
  2. Donis-Keller H. Phy M: an RNase activity specific for U and A residues useful in RNA sequence analysis. Nucleic Acids Res. 1980 Jul 25;8(14):3133–3142. doi: 10.1093/nar/8.14.3133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Erdmann V. A. Collection of published 5S and 5.8S ribosomal RNA sequences. Nucleic Acids Res. 1978 Jan;5(1):r1–r13. [PMC free article] [PubMed] [Google Scholar]
  4. Feunteun J., Jordan B. R., Monier R. Study of the maturation of 5 s RNA precursors in Escherichia coli. J Mol Biol. 1972 Oct 14;70(3):465–474. doi: 10.1016/0022-2836(72)90553-0. [DOI] [PubMed] [Google Scholar]
  5. Geyl D., Böck A., Isono K. An improved method for two-dimensional gel-electrophoresis: analysis of mutationally altered ribosomal proteins of Escherichia coli. Mol Gen Genet. 1981;181(3):309–312. doi: 10.1007/BF00425603. [DOI] [PubMed] [Google Scholar]
  6. Gray G. L., Mainzer S. E., Rey M. W., Lamsa M. H., Kindle K. L., Carmona C., Requadt C. Structural genes encoding the thermophilic alpha-amylases of Bacillus stearothermophilus and Bacillus licheniformis. J Bacteriol. 1986 May;166(2):635–643. doi: 10.1128/jb.166.2.635-643.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hori H. Evolution of 5sRNA. J Mol Evol. 1975 Dec 31;7(1):75–86. doi: 10.1007/BF01732181. [DOI] [PubMed] [Google Scholar]
  8. Hori H., Osawa S. Evolutionary change in 5S RNA secondary structure and a phylogenic tree of 54 5S RNA species. Proc Natl Acad Sci U S A. 1979 Jan;76(1):381–385. doi: 10.1073/pnas.76.1.381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ihara H., Sasaki T., Tsuboi A., Yamagata H., Tsukagoshi N., Udaka S. Complete nucleotide sequence of a thermophilic alpha-amylase gene: homology between prokaryotic and eukaryotic alpha-amylases at the active sites. J Biochem. 1985 Jul;98(1):95–103. doi: 10.1093/oxfordjournals.jbchem.a135279. [DOI] [PubMed] [Google Scholar]
  10. Isono K. A computer program package for storing and retrieving DNA/RNA and protein sequence data. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):101–112. doi: 10.1093/nar/12.1part1.101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Isono K. Computer programs to analyze DNA and amino acid sequence data. Nucleic Acids Res. 1982 Jan 11;10(1):85–89. doi: 10.1093/nar/10.1.85. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Isono S., Isono K. Mutations affecting the structural genes and the genes coding for modifying enzymes for ribosomal proteins in Escherichia coli. Mol Gen Genet. 1978 Sep 20;165(1):15–20. doi: 10.1007/BF00270371. [DOI] [PubMed] [Google Scholar]
  13. Kawazu T., Nakanishi Y., Uozumi N., Sasaki T., Yamagata H., Tsukagoshi N., Udaka S. Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa beta-amylase. J Bacteriol. 1987 Apr;169(4):1564–1570. doi: 10.1128/jb.169.4.1564-1570.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kimura M., Ohta T. Eukaryotes-prokaryotes divergence estimated by 5S ribosomal RNA sequences. Nat New Biol. 1973 Jun 13;243(128):199–200. doi: 10.1038/newbio243199a0. [DOI] [PubMed] [Google Scholar]
  15. Marotta C. A., Varricchio F., Smith I., Weissman S. M. The primary structure of Bacillus subtilis and Bacillus stearothermophilus 5 S ribonucleic acids. J Biol Chem. 1976 May 25;251(10):3122–3127. [PubMed] [Google Scholar]
  16. Matsuura Y., Kusunoki M., Harada W., Kakudo M. Structure and possible catalytic residues of Taka-amylase A. J Biochem. 1984 Mar;95(3):697–702. doi: 10.1093/oxfordjournals.jbchem.a134659. [DOI] [PubMed] [Google Scholar]
  17. Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
  18. Mielenz J. R. Bacillus stearothermophilus contains a plasmid-borne gene for alpha-amylase. Proc Natl Acad Sci U S A. 1983 Oct;80(19):5975–5979. doi: 10.1073/pnas.80.19.5975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mori M., Tanimoto A., Yoda K., Harada S., Koyama N., Hashiguchi K., Obinata M., Yamasaki M., Tamura G. Essential structure in the cloned transforming DNA that induces gene amplification of the Bacillus subtilis amyE-tmrB region. J Bacteriol. 1986 Jun;166(3):787–794. doi: 10.1128/jb.166.3.787-794.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Nakajima R., Imanaka T., Aiba S. Nucleotide sequence of the Bacillus stearothermophilus alpha-amylase gene. J Bacteriol. 1985 Jul;163(1):401–406. doi: 10.1128/jb.163.1.401-406.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nishizawa M., Ozawa F., Hishinuma F. Molecular cloning of an amylase gene of Bacillus circulans. DNA. 1987 Jun;6(3):255–265. doi: 10.1089/dna.1987.6.255. [DOI] [PubMed] [Google Scholar]
  22. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  23. SAITO H., MIURA K. I. PREPARATION OF TRANSFORMING DEOXYRIBONUCLEIC ACID BY PHENOL TREATMENT. Biochim Biophys Acta. 1963 Aug 20;72:619–629. [PubMed] [Google Scholar]
  24. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  26. Takkinen K., Pettersson R. F., Kalkkinen N., Palva I., Söderlund H., Käriäinen L. Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J Biol Chem. 1983 Jan 25;258(2):1007–1013. [PubMed] [Google Scholar]
  27. Tsukagoshi N., Ihara H., Yamagata H., Udaka S. Cloning and expression of a thermophilic alpha-amylase gene from Bacillus stearothermophilus in Escherichia coli. Mol Gen Genet. 1984;193(1):58–63. doi: 10.1007/BF00327414. [DOI] [PubMed] [Google Scholar]
  28. Yamazaki H., Ohmura K., Nakayama A., Takeichi Y., Otozai K., Yamasaki M., Tamura G., Yamane K. Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing Bacillus subtilis strain: molecular cloning and nucleotide sequences. J Bacteriol. 1983 Oct;156(1):327–337. doi: 10.1128/jb.156.1.327-337.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Yang M., Galizzi A., Henner D. Nucleotide sequence of the amylase gene from Bacillus subtilis. Nucleic Acids Res. 1983 Jan 25;11(2):237–249. doi: 10.1093/nar/11.2.237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES