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. 1988 Jun;170(6):2873–2878. doi: 10.1128/jb.170.6.2873-2878.1988

Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene.

H M Lim 1, J J Pène 1, R W Shaw 1
PMCID: PMC211218  PMID: 3131315

Abstract

Two forms of heat-stable, zinc-containing beta-lactamase II have been described for strains of Bacillus cereus and have been shown to differ in substrate specificity (R. B. Davies, E. P. Abraham, J. Fleming, and M. R. Pollock, Biochem. J. 145: 409-411, 1975). We report here the nucleotide sequence, inferred amino acid sequence, and expression of beta-lactamase II from B. cereus 5/B/6 and compare our results with those for its homolog characterized in B. cereus 569/H (M. Hussain, C. Anthony, M. J. Madonna, and J. O. Lampen, J. Bacteriol. 164: 223-229, 1985) to document amino acid differences contributing to the specific properties of these enzymes.

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Selected References

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

  1. Ambler R. P., Daniel M., Fleming J., Hermoso J. M., Pang C., Waley S. G. The amino acid sequence of the zinc-requiring beta-lactamase II from the bacterium Bacillus cereus 569. FEBS Lett. 1985 Sep 23;189(2):207–211. doi: 10.1016/0014-5793(85)81024-3. [DOI] [PubMed] [Google Scholar]
  2. Chen E. Y., Seeburg P. H. Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA. 1985 Apr;4(2):165–170. doi: 10.1089/dna.1985.4.165. [DOI] [PubMed] [Google Scholar]
  3. Connolly A. K., Waley S. G. Characterization of the membrane beta-lactamase in Bacillus cereus 569/H/9. Biochemistry. 1983 Sep 27;22(20):4647–4651. doi: 10.1021/bi00289a006. [DOI] [PubMed] [Google Scholar]
  4. Contente S., Dubnau D. Characterization of plasmid transformation in Bacillus subtilis: kinetic properties and the effect of DNA conformation. Mol Gen Genet. 1979 Jan 2;167(3):251–258. doi: 10.1007/BF00267416. [DOI] [PubMed] [Google Scholar]
  5. Davies R. B. Comparison of beta-lactamase II from Bacillus cereus 569/H/9 with a beta-lactamase from Bacillus cereus 5/B/6. Biochem J. 1975 Feb;145(2):409–411. doi: 10.1042/bj1450409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Guo L. H., Wu R. New rapid methods for DNA sequencing based in exonuclease III digestion followed by repair synthesis. Nucleic Acids Res. 1982 Mar 25;10(6):2065–2084. doi: 10.1093/nar/10.6.2065. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Henikoff S. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene. 1984 Jun;28(3):351–359. doi: 10.1016/0378-1119(84)90153-7. [DOI] [PubMed] [Google Scholar]
  8. Hussain M., Carlino A., Madonna M. J., Lampen J. O. Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J Bacteriol. 1985 Oct;164(1):223–229. doi: 10.1128/jb.164.1.223-229.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hussain M., Pastor F. I., Lampen J. O. Cloning and sequencing of the blaZ gene encoding beta-lactamase III, a lipoprotein of Bacillus cereus 569/H. J Bacteriol. 1987 Feb;169(2):579–586. doi: 10.1128/jb.169.2.579-586.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Little C., Emanuel E. L., Gagnon J., Waley S. G. Identification of an essential glutamic acid residue in beta-lactamase II from Bacillus cereus. Biochem J. 1986 Jan 15;233(2):465–469. doi: 10.1042/bj2330465. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Madgwick P. J., Waley S. G. beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis. Biochem J. 1987 Dec 15;248(3):657–662. doi: 10.1042/bj2480657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Madonna M. J., Zhu Y. F., Lampen J. O. Nucleotide sequence of the beta-lactamase I gene of Bacillus cereus strains 569/H and 5/B. Nucleic Acids Res. 1987 Feb 25;15(4):1877–1877. doi: 10.1093/nar/15.4.1877. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. Nielsen J. B., Lampen J. O. Beta-lactamase III of Bacillus cereus 569: membrane lipoprotein and secreted protein. Biochemistry. 1983 Sep 27;22(20):4652–4656. doi: 10.1021/bi00289a007. [DOI] [PubMed] [Google Scholar]
  15. Ostroff G. R., Pène J. J. Molecular cloning with bifunctional plasmid vectors in Bacillus subtilis. I. Construction and analysis of B. subtilis clone banks in Escherichia coli. Mol Gen Genet. 1984;193(2):299–305. doi: 10.1007/BF00330684. [DOI] [PubMed] [Google Scholar]
  16. Ostroff G. R., Pène J. J. Molecular cloning with bifunctional plasmid vectors in Bacillus subtilis. II. Transfer of sequences propagated in Escherichia coli to B. subtilis. Mol Gen Genet. 1984;193(2):306–311. doi: 10.1007/BF00330685. [DOI] [PubMed] [Google Scholar]
  17. Ostroff G. R., Pène J. J. Molecular cloning with bifunctional plasmid vectors in Bacillus subtilis: isolation of a spontaneous mutant of Bacillus subtilis with enhanced transformability for Escherichia coli-propagated chimeric plasmid DNA. J Bacteriol. 1983 Nov;156(2):934–936. doi: 10.1128/jb.156.2.934-936.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. POLLOCK M. R. The cell-bound penicillinase of Bacillus cereus. J Gen Microbiol. 1956 Aug;15(1):154–169. doi: 10.1099/00221287-15-1-154. [DOI] [PubMed] [Google Scholar]
  19. Peterson G. L. Determination of total protein. Methods Enzymol. 1983;91:95–119. doi: 10.1016/s0076-6879(83)91014-5. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sloma A., Gross M. Molecular cloning and nucleotide sequence of the type I beta-lactamase gene from Bacillus cereus. Nucleic Acids Res. 1983 Jul 25;11(14):4997–5004. doi: 10.1093/nar/11.14.4997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Struhl K., Cameron J. R., Davis R. W. Functional genetic expression of eukaryotic DNA in Escherichia coli. Proc Natl Acad Sci U S A. 1976 May;73(5):1471–1475. doi: 10.1073/pnas.73.5.1471. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Sutton B. J., Artymiuk P. J., Cordero-Borboa A. E., Little C., Phillips D. C., Waley S. G. An X-ray-crystallographic study of beta-lactamase II from Bacillus cereus at 0.35 nm resolution. Biochem J. 1987 Nov 15;248(1):181–188. doi: 10.1042/bj2480181. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Wang W., Mézes P. S., Yang Y. Q., Blacher R. W., Lampen J. O. Cloning and sequencing of the beta-lactamase I gene of Bacillus cereus 5/B and its expression in Bacillus subtilis. J Bacteriol. 1985 Aug;163(2):487–492. doi: 10.1128/jb.163.2.487-492.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. West R. W., Jr, Rodriguez R. L. Construction and characterization of E. coli promoter-probe plasmid vectors. III. pBR322 derivatives with deletions in the tetracycline resistance promoter region. Gene. 1982 Dec;20(2):291–304. doi: 10.1016/0378-1119(82)90047-6. [DOI] [PubMed] [Google Scholar]
  27. von Heijne G. How signal sequences maintain cleavage specificity. J Mol Biol. 1984 Feb 25;173(2):243–251. doi: 10.1016/0022-2836(84)90192-x. [DOI] [PubMed] [Google Scholar]
  28. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

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