The role of the outer membrane in formaldehyde tolerance in Escherichia coli VU3695 and Halomonas sp. MAC

References

1. Azachi M., Henis Y., Oren A., f Gurevich P., Sarig S. Transformation of formaldehyde bv a Halomonas sp. Can J Microbiol 1995; 41:548–553
   [Google Scholar]
2. Birnboim H.C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 1979; 7:1513–1523
   [Google Scholar]
3. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem 1976; 72:248–254
   [Google Scholar]
4. Diver M.D., Larry E.B., Pamela A.S. Transformation of Pseudomonas aeruginosa by electroporation. Anal Biochem 1990; 189:75–79
   [Google Scholar]
5. Hancock R.E.W., Carey A.M. Outer membrane of Pseudomonas aeruginosa: heat and 2-mercaptoethanol-modifiable proteins. J Bacteriol 1979; 140:902–910
   [Google Scholar]
6. Hancock R.E.W., Nikaido H. Outer membranes of gramnegative bacteria XIX. Isolation from Pseudomonas aeruginosa PAOl and use in reconstitution and definition of the permeability barrier. J Bacteriol 1978; 136:381–390
   [Google Scholar]
7. Kato N., Kobayashi H., Shimao M., Sakazawa C. Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61. Agric Biol Chem 1984; 48:2017–2023
   [Google Scholar]
8. Kato N., Yamagami N., Shimao M., Sakazawa C. Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61. Eur J Biochem 1986; 156:59–64
   [Google Scholar]
9. Kato N., Miyamoto N., Shimao M., Sakazawa C. 3-Hexulose phosphate synthase from a new facultative methylotroph, Mycobacterium gastri MB19. Agric Biol Chem 1988; 52:2659–2661
   [Google Scholar]
10. Kaulfers P.M., Brandt D. Isolation of a conjugative plasmid in Escherichia coli determining formaldehyde resistance. FEMS Microbiol Eett 1987; 43:161–163
    [Google Scholar]
11. Kaulfers P.M., Laufs R. Übertragbare Formaldehydresistenz bei Serratia marcescens. Zentralbl Bakteriol Mikrobiol Hyg 1 Abt OrigB 1985; 181:309–319
    [Google Scholar]
12. Kaulfers P., M. & Marquardt A. Demonstration of formaldehyde dehydrogenase activity in formaldehyde-resistant Enterobacteriaceae. FEMS Microbiol Lett 1991; 79:335–338
    [Google Scholar]
13. Lidstrom M.E. The aerobic methylotrophic bacteria. In The Prokaryotes. A Handbook on the Biology of Bacteria: Ecophysiology 1992 Edited by Balows A., Triiper H.G., Dworkin M., Harder W., Schleifer K.-H. New York: Springer-Verlag; Isolation, Identification, Applications, pp 431–445
    [Google Scholar]
14. Lieve L. The barrier function of the gram-negative cell envelope. Al#« NY Acad Sci 1974; 235:109–127
    [Google Scholar]
15. McGavin M., Lam J., Forsberg C.W. Regulation and distribution of Fibrobacter succinogenes subsp succinogenes S85 endo-glucanases. Appl Environ Microbiol 1990; 56:1235–1244
    [Google Scholar]
16. Nikaido H., Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev 1985; 49:1–32
    [Google Scholar]
17. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning: a Laboratory Manual, 2nd edn 1989 Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
18. Spicer A.B., Spooner D.F. The inhibition of growth of Escherichia coli spheroplasts by antibacterial agents. J Gen Microbiol 1974; 80:37–50
    [Google Scholar]
19. Wang W., Thomson J.A. Nucleotide sequence of the cel A gene encoding a cellodextrinase of R uminococcus flavefaciens. Mol Gen Genet 1990; 222:265–269
    [Google Scholar]
20. Weiser R., Asscher A.W., Wimpenny J. In vitro reversal of antibiotic resistance by ethylendiamine tetraacetic acid. Nature 1968; 219:1365–1366
    [Google Scholar]