Evidence for Movement of the Alpha-amylase Gene into Two Phylogenetically Distant Bacillus Stearothermophilus Strains

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1988 Mar 1

PMID 3257753

Citations 1

Authors

H Satoh

H Nishida

K Isono

Affiliations

Soon will be listed here.

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.

Citing Articles

Cloning and sequencing of the gene encoding thermophilic beta-amylase of Clostridium thermosulfurogenes.

Kitamoto N, Yamagata H, Kato T, Tsukagoshi N, Udaka S J Bacteriol. 1988; 170(12):5848-54.

PMID: 2461360 PMC: 211691. DOI: 10.1128/jb.170.12.5848-5854.1988.

References

Brownlee G, SANGER F . Nucleotide sequences from the low molecular weight ribosomal RNA of Escherichia coli. J Mol Biol. 1967; 23(3):337-53. DOI: 10.1016/s0022-2836(67)80109-8. View

Saito H, MIURA K . PREPARATION OF TRANSFORMING DEOXYRIBONUCLEIC ACID BY PHENOL TREATMENT. Biochim Biophys Acta. 1963; 72:619-29. View

Kimura M, Ohta T . Eukaryotes-prokaryotes divergence estimated by 5S ribosomal RNA sequences. Nat New Biol. 1973; 243(128):199-200. DOI: 10.1038/newbio243199a0. View

Southern E . Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975; 98(3):503-17. DOI: 10.1016/s0022-2836(75)80083-0. View

Hori H . Evolution of 5sRNA. J Mol Evol. 1975; 7(1):75-86. DOI: 10.1007/BF01732181. View

Marotta C, Varricchio F, Smith I, Weissman S . The primary structure of Bacillus subtilis and Bacillus stearothermophilus 5 S ribonucleic acids. J Biol Chem. 1976; 251(10):3122-7. View

Rigby P, 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; 113(1):237-51. DOI: 10.1016/0022-2836(77)90052-3. View

SANGER F, Nicklen S, Coulson A . DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977; 74(12):5463-7. PMC: 431765. DOI: 10.1073/pnas.74.12.5463. View

Erdmann V . Collection of published 5S and 5.8S ribosomal RNA sequences. Nucleic Acids Res. 1978; 5(1):r1-r13. PMC: 341980. View

10.

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; 165(1):15-20. DOI: 10.1007/BF00270371. View

11.

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; 76(1):381-5. PMC: 382943. DOI: 10.1073/pnas.76.1.381. View

12.

Donis-Keller H . Phy M: an RNase activity specific for U and A residues useful in RNA sequence analysis. Nucleic Acids Res. 1980; 8(14):3133-42. PMC: 324360. DOI: 10.1093/nar/8.14.3133. View

13.

Geyl D, Bock 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):309-12. DOI: 10.1007/BF00425603. View

14.

Isono K . Computer programs to analyze DNA and amino acid sequence data. Nucleic Acids Res. 1982; 10(1):85-9. PMC: 326116. DOI: 10.1093/nar/10.1.85. View

15.

Takkinen K, Pettersson R, Kalkkinen N, PALVA I, Soderlund H, Kaariainen L . Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J Biol Chem. 1983; 258(2):1007-13. View

16.

Yang M, Galizzi A, Henner D . Nucleotide sequence of the amylase gene from Bacillus subtilis. Nucleic Acids Res. 1983; 11(2):237-49. PMC: 325711. DOI: 10.1093/nar/11.2.237. View

17.

Messing J . New M13 vectors for cloning. Methods Enzymol. 1983; 101:20-78. DOI: 10.1016/0076-6879(83)01005-8. View

18.

Mielenz J . Bacillus stearothermophilus contains a plasmid-borne gene for alpha-amylase. Proc Natl Acad Sci U S A. 1983; 80(19):5975-9. PMC: 390200. DOI: 10.1073/pnas.80.19.5975. View

19.

Yamazaki H, Ohmura K, Nakayama A, Takeichi Y, OTOZAI K, Yamasaki M . Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing Bacillus subtilis strain: molecular cloning and nucleotide sequences. J Bacteriol. 1983; 156(1):327-37. PMC: 215086. DOI: 10.1128/jb.156.1.327-337.1983. View

20.

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. View