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. 1987 Dec;84(23):8530–8534. doi: 10.1073/pnas.84.23.8530

Characterization of pHV2 from Halobacterium volcanii and its use in demonstrating transformation of an archaebacterium.

R L Charlebois 1, W L Lam 1, S W Cline 1, W F Doolittle 1
PMCID: PMC299578  PMID: 2825193

Abstract

We determined the complete nucleotide sequence of the 6354-base-pair plasmid pHV2 of the archaebacterium Halobacterium volcanii. This plasmid is present in approximately six copies per chromosome. We have generated a strain, H. volcanii WFD11, cured of pHV2 by treatment of liquid cultures with ethidium bromide. We describe PEG-mediated transformation of H. volcanii WFD11 with intact pHV2 and with a form of pHV2 marked by a 93-base-pair deletion generated in vitro.

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Selected References

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  1. Bayley S. T., Morton R. A. Recent developments in the molecular biology of extremely halophilic bacteria. CRC Crit Rev Microbiol. 1978;6(2):151–205. doi: 10.3109/10408417809090622. [DOI] [PubMed] [Google Scholar]
  2. Bertani G., Baresi L. Genetic transformation in the methanogen Methanococcus voltae PS. J Bacteriol. 1987 Jun;169(6):2730–2738. doi: 10.1128/jb.169.6.2730-2738.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blanck A., Oesterhelt D. The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin. EMBO J. 1987 Jan;6(1):265–273. doi: 10.1002/j.1460-2075.1987.tb04749.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cline S. W., Doolittle W. F. Efficient transfection of the archaebacterium Halobacterium halobium. J Bacteriol. 1987 Mar;169(3):1341–1344. doi: 10.1128/jb.169.3.1341-1344.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Daniels C. J., McKee A. H., Doolittle W. F. Archaebacterial heat-shock proteins. EMBO J. 1984 Apr;3(4):745–749. doi: 10.1002/j.1460-2075.1984.tb01878.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dennis P. P. Molecular biology of archaebacteria. J Bacteriol. 1986 Nov;168(2):471–478. doi: 10.1128/jb.168.2.471-478.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Guo L. H., Yang R. C., Wu R. An improved strategy for rapid direct sequencing of both strands of long DNA molecules cloned in a plasmid. Nucleic Acids Res. 1983 Aug 25;11(16):5521–5540. doi: 10.1093/nar/11.16.5521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Jones W. J., Nagle D. P., Jr, Whitman W. B. Methanogens and the diversity of archaebacteria. Microbiol Rev. 1987 Mar;51(1):135–177. doi: 10.1128/mr.51.1.135-177.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Korn L. J., Queen C. L., Wegman M. N. Computer analysis of nucleic acid regulatory sequences. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4401–4405. doi: 10.1073/pnas.74.10.4401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mescher M. F., Strominger J. L. Structural (shape-maintaining) role of the cell surface glycoprotein of Halobacterium salinarium. Proc Natl Acad Sci U S A. 1976 Aug;73(8):2687–2691. doi: 10.1073/pnas.73.8.2687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Mevarech M., Werczberger R. Genetic transfer in Halobacterium volcanii. J Bacteriol. 1985 Apr;162(1):461–462. doi: 10.1128/jb.162.1.461-462.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mullakhanbhai M. F., Larsen H. Halobacterium volcanii spec. nov., a Dead Sea halobacterium with a moderate salt requirement. Arch Microbiol. 1975 Aug 28;104(3):207–214. doi: 10.1007/BF00447326. [DOI] [PubMed] [Google Scholar]
  15. Patterson N. H., Pauling C. Evidence for two restriction-modification systems in Halobacterium cutirubrum. J Bacteriol. 1985 Aug;163(2):783–784. doi: 10.1128/jb.163.2.783-784.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pfeifer F., Weidinger G., Goebel W. Characterization of plasmids in halobacteria. J Bacteriol. 1981 Jan;145(1):369–374. doi: 10.1128/jb.145.1.369-374.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Sapienza C., Doolittle W. F. Unusual physical organization of the Halobacterium genome. Nature. 1982 Feb 4;295(5848):384–389. doi: 10.1038/295384a0. [DOI] [PubMed] [Google Scholar]
  18. Schnabel H., Zillig W., Pfäffle M., Schnabel R., Michel H., Delius H. Halobacterium halobium phage øH. EMBO J. 1982;1(1):87–92. doi: 10.1002/j.1460-2075.1982.tb01129.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Shepherd J. C. Method to determine the reading frame of a protein from the purine/pyrimidine genome sequence and its possible evolutionary justification. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1596–1600. doi: 10.1073/pnas.78.3.1596. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Thompson J. A., Blakesley R. W., Doran K., Hough C. J., Wells R. D. Purification of nucleic acids by RPC-5 ANALOG chromatography: peristaltic and gravity-flow applications. Methods Enzymol. 1983;100:368–399. doi: 10.1016/0076-6879(83)00068-3. [DOI] [PubMed] [Google Scholar]
  21. Toeckenius W., Kunau W. H. Further characterization of particulate fractions from lysed cell envelopes of Halobacterium halobium and isolation of gas vacuole membranes. J Cell Biol. 1968 Aug;38(2):337–357. doi: 10.1083/jcb.38.2.337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tramontano A., Macchiato M. F. Probability of coding of a DNA sequence: an algorithm to predict translated reading frames from their thermodynamic characteristics. Nucleic Acids Res. 1986 Jan 10;14(1):127–135. doi: 10.1093/nar/14.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Walseth T. F., Johnson R. A. The enzymatic preparation of [alpha-(32)P]nucleoside triphosphates, cyclic [32P] AMP, and cyclic [32P] GMP. Biochim Biophys Acta. 1979 Mar 28;562(1):11–31. doi: 10.1016/0005-2787(79)90122-9. [DOI] [PubMed] [Google Scholar]
  24. Woese C. R., Fox G. E. Phylogenetic structure of the prokaryotic domain: the primary kingdoms. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5088–5090. doi: 10.1073/pnas.74.11.5088. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Woese C. R., Magrum L. J., Fox G. E. Archaebacteria. J Mol Evol. 1978 Aug 2;11(3):245–251. doi: 10.1007/BF01734485. [DOI] [PubMed] [Google Scholar]
  26. 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]

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