Isolation, sequence, and expression of the gene encoding halocin H4, a bacteriocin from the halophilic archaeon Haloferax mediterranei R4

Journal of Bacteriology

Volumn 179, Issue 2, 1997, Pages 548-551

  Cheung, Joyce ^a,b   Danna, Kathleen J ^a,c   O'Connor, Elizabeth M ^a   Price, Lance B ^a   Shand, Richard F ^a  

^a NORTHERN ARIZONA UNIVERSITY   (United States)

^b ARIZONA STATE UNIVERSITY   (United States)

^c UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCIN;

ARTICLE; GENE EXPRESSION; GENE ISOLATION; GENE SEQUENCE; HALOBACTERIUM; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL;

EID: 0031036328     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.2.548-551.1997     Document Type: Article

References (34)

1. American Type Culture Collection. 1989. Catalogue of bacteria and bacteriophages, p. 336, 17th ed. American Type Culture Collection, Rockville, Md.
2. Barefoot, S. F., K. M. Harmon, D. A. Grinstead, and C. G. Nettles. 1992. Bacteriocins, molecular biology, p. 191-202. In J. Lederberg (ed.), Encyclopedia of microbiology, vol. 1. Academic Press, Inc., New York.
3. Betlach, M. C., J. Friedman, H. W. Boyer, and F. Pfeifer. 1984. Characterization of a halobacterial gene affecting bacterio-opsin gene expression. Nucleic Acids Res. 20:7949-7950.
4. Betlach, M. C., and F. Rodriguez-Valera. Unpublished data.
5. Blanck, A., and D. Oesterhelt. 1987. The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin. EMBO J. 6:265-273.
6. Braun, V., H. Pilsl, and P. Groß. 1994. Colicins: structures, mode of action, transfer through membranes, and evolution. Arch. Microbiol. 161:199-206.
7. DasSarma, S., U. L. RajBhundary, and H. G. Khorana. 1984. Bacterio-opsin mRNA in wild-type and bacterio-opsin-deficient Halobacterium halobium strains. Proc. Natl. Acad. Sci. USA 81:125-129.
8. Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction fragments to high specific activity. Anal. Biochem, 132:6-13.
9. Gropp, F., R. Gropp, and M. C. Betlach. 1994. A fourth gene in the bop gene cluster of Halobacterium halobium is co-regulated with the bop gene. System. Appl. Microbiol. 16:716-724.
10. Hightower, R. C., and D. V. Santi. 1989. Migration properties of circular DNAs using orthogonal-field-alteration gel electrophoresis. Electrophoresis 10:283-290.
11. Izard, J. W., and D. A. Kendall. 1994. Signal peptides: exquisitely designed transport promoters. Mol. Microbiol. 13:765-773.
12. Jack, R. W., J. R. Tagg, and B. Ray. 1995. Bacteriocins of gram-positive bacteria. Microbiol. Rev. 59:171-200.
13. Kamekura, M., Y. Seno, M. L. Holmes, and M. L. Dyall-Smith. 1992. Molecular cloning and sequencing of the gone for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii. J. Bacteriol. 174:736-742.
14. López-García, P., J. P. Abad, C. Smith, and R. Amils. 1992. Genomic organization of the halophilic archaeon Haloferax maditerranei: physical map of the chromosome. Nucleic Acids Res. 20:2459-2464.
15. Meseguer, I., and F. Rodriguez-Valera. 1985. Production and purification of halocin H4. FFMS Microbiol. Lett. 28:177-182.
16. Meseguer, I., und F. Rodriguez-Valera. 1986. Effect of halocin H4 on cells of Halobacterium halobium. J. Gen. Microbiol. 132:3061-3068.
17. Meseguer, I., F. Rodriguez-Valera, and A. Ventosa. 1986. Antagonistic interactions among halobacteria due to halocin production. FEMS Microbiol. Lett. 36:177-182.
18. Mickel, S., V. Arena, and W. Bauer. 1977. Physical properties and gel electrophoresis behavior of R12-derived plasmid DNA. Nucleic Acids Res. 4:1465.
19. Miller, J. H. 1977. Experiments in molecular genetics, p. 433, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
20. Moritz, A., B. Lankat-Buttgereit, H. Gross, and W. Goebel. 1985. Common structural features of the genes for two stable RNAs from Halobacterium halobium. Nucleic Acids Res. 13:31-43.
21. O'Connor, E. M., L. B. Price, and R. F. Shand. Unpublished data.
22. Palmer, J. R., and C. J. Daniels. 1995. In vivo definition of an archaeal promoter. J. Bacteriol. 177:1844-1849.
23. Rdest, U., and M. Strum. 1987. Bacteriocins from halobacteria, p. 271-278. In R. Burgess (ed.), Protein purification: micro to macro. Alan R. Lisa, Inc., New York.
24. Rodriguez-Valera, F., G. Juez, and D. J. Kushner. 1982. Halocins: salt- dependent bacteriocins produced by extremely halophilic rods. Can. J. Microbiol. 28:151-154.
25. Ruepp, A., and J. Soppa. 1996. Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products and transcripts of the arcRABC gene cluster. J. Bacteriol. 178:4942- 4947.
26. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, p. 7.79-7.83, B.23., 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
27. Sanchez, R. S. (Universidad de Salamanca). 1994. Personal communication.
28. Shand, R. F., and M. C. Betlach. 1991. Expression of the bop gene cluster of Halobacterium halobium is induced by low oxygen tension and by light. J. Bacteriol. 173:4692-4699.
29. Skvirsky, R. 1996. Personal communication.
30. Torreblanca, M., I. Meseguer, and F. Rodriguez-Valera. 1989. Halocin H6, a bacteriocin from Haloferax gibbonsii. J. Gen. Microbiol. 135:2655-2661.
31. Torreblunea, M., I. Meseguer, and F. Rodriguez-Valera. 1990. Effects of halocin H6 on the morphology of sensitive cells. Biochem. Cell Biol. 68:396- 399.
32. Torreblanca, M., I. Meseguer, and A. Ventosa. 1994. Production of halocin is a practically universal feature of archaeal halophilic rods. Lett. Appl. Microbiol. 19:201-205.
33. Vining, L. C. 1995. Genetic and environmental control of antibiotic production, p. 1-7. In L. C. Vining and C. Stuttard (ed.), Genetics and biochemistry of antibiotic production. Butterworth-Heinemann, Newton, Mass.
34. von Heijne, G. 1984. How signal sequences maintain cleavage specificity. J. Mol. Biol. 173:243-251.