Genetic analysis of microcin H47 immunity

Canadian Journal of Microbiology

Volumn 44, Issue 7, 1998, Pages 692-697

  Rodríguez, Eliana ^a   Laviña, Magela ^a  

^a Institute Cle fi'Sica   (Uruguay)

Author keywords

Membrane peptide; Microcin H47; Microcin immunity; PhoA gene fusion

Indexed keywords

BACTERICIDE; MICROCIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; DRUG MANUFACTURE; ESCHERICHIA COLI; GENE FUSION; GENE LOCUS; GENETIC ANALYSIS; GENETIC CODE; GENETIC COMPLEMENTATION; IMMUNITY; MUTAGENICITY; OPERON; PRIORITY JOURNAL;

ESCHERICHIA COLI;

EID: 0031763742     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/w98-044     Document Type: Article

References (22)

1. Berg, C.M., Berg, D.E., and Groisman, A. 1989. Transposable elements and the genetic engineering of bacteria. In Mobile DNA. Edited by D.E. Berg and M.M. Howe. American Society for Microbiology. Washington, D.C. pp. 879-926.
2. Boyd, D., Manoil, C., and Beckwith, J. 1987. Determinants of membrane protein topology. Proc. Natl. Acad. Sci. U.S.A. 84: 8525-8529.
3. Brickman, E., and Beckwith, J. 1975. Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and Φ80 transducing phages. J. Mol. Biol. 96: 307-316.
4. Claros, M.G., and von Heijne, G. 1994. TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10: 685-686.
5. de Vos, W.M., Kuipers, O.P., van der Meer, J.R., and Siezen, R.J. 1995. Maturation pathway of nisin and other lantibiotics: posttranslationally modified antimicrobial peptides exported by Gram-positive bacteria. Mol. Microbiol. 17: 427-437.
6. Espesset, D., Piet, P., Lazdunski, C., and Géli, V. 1994. Immunity proteins to pore-forming colicins: structure-function relationships. Mol. Microbiol. 13: 1111-1120.
7. Path, M.J., Skvirsky, R., Gilson, L., Mahanty, H.K., and Kolter, R. 1992. The secretion of colicin V. In Bacteriocins, microcins, and lantibiotics. Edited by R. James, F. Lazdunski, and F. Pattus. Springer-Verlag KG, Heidelberg, Germany, pp. 331-348.
8. Gaggero, C., Moreno, F., and Laviña, M. 1993. Genetic analysis of microcin H47 antibiotic system. J. Bacteriol. 175: 5420-5427.
9. Gutiérrez, C., Barondess, J., Manoil, C., and Beckwith, J. 1987. The use of transposon TnphoA to detect genes for cell envelope proteins subject to a common regulatory stimulus. J. Mol. Biol. 195: 289-297.
10. Kleckner, N., Bender, J., and Gottesman, S. 1992. Tn/0 and other transposons. Methods Enzymol. 204: 139-180.
11. Klein, P., Kanehisa, M., and DeLisi, C. 1985. The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta, 815: 468-476.
12. Kolter, R., and Moreno, F. 1992. Genetics of ribosomally synthesized peptide antibiotics. Annu. Rev. Microbiol. 46: 141-164.
13. Kyte, J., and Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132.
14. Laviña, M., and Gaggero, C. 1992. Genetic determinants for microcin H47, an Escherichia coli chromosome-encoded antibiotic. In Bacteriocins, microcins, and lantibiotics. Edited by R. James, F. Lazdunski, and F. Pattus. Springer-Verlag KG, Heidelberg, Germany, pp. 413-416.
15. Laviña, M., Gaggero, C., and Moreno, F. 1990. Microcin H47, a chromosome-encoded microcin antibiotic of Escherichia coli. J. Bacteriol. 172: 6585-6588.
16. Manoil, C., and Beckwith, J. 1985. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. U.S.A. 82: 8129-8133.
17. Miller, J.H. 1992. β-Galactosidase assay. In A short course in bacterial genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. pp. 72-74.
18. Rao, J.K.M., and Argos, P. 1986. A conformational preference parameter to predict helices in integral membrane proteins. Biochim. Biophys. Acta, 869: 197-214.
19. Sanger, F., Nicklen, S., and Coulson, A.R. 1977. DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A. 74: 5463-5467.
20. San Millán, J.L., Boyd, D., Dalbey, R., Wickner, W., and Beckwith, J. 1989. Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase. J. Bacteriol. 171: 5536-5541.
21. von Heijne, G. 1986a. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14: 4683-4690.
22. von Heijne, G. 1986b. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5: 3021-3027.