Characterization of Enterococcus faecalis alkaline phosphatase and use in identifying Streptococcus agalactiae secreted proteins

Journal of Bacteriology

Volumn 181, Issue 18, 1999, Pages 5790-5799

  Lee, Martin H ^a   Nittayajarn, Aphakorn ^a   Ross, R Paul ^b,c   Rothschild, Cynthia B ^b   Parsonage, Derek ^b   Claiborne, Al ^b   Rubens, Craig E ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b WAKE FOREST BAPTIST HEALTH   (United States)

^c ANIMAL AND GRASSLAND RESEARCH AND INNOVATION CENTRE   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; CELL MEMBRANE PROTEIN; CHIMERIC PROTEIN; CHROMOGENIC SUBSTRATE; GENE PRODUCT; LACTOSE PERMEASE; MEMBRANE PROTEIN; PEPTIDASE; SIGNAL PEPTIDE;

ARTICLE; BACILLUS SUBTILIS; CONTROLLED STUDY; DELETION MUTANT; ENTEROCOCCUS FAECALIS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME LOCALIZATION; ESCHERICHIA COLI; GRAM POSITIVE BACTERIUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; SEQUENCE HOMOLOGY; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS GROUP A; STREPTOCOCCUS PYOGENES;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ENTEROCOCCUS FAECALIS; ESCHERICHIA COLI; POSIBACTERIA; STREPTOCOCCUS AGALACTIAE; STREPTOCOCCUS GROUP A; STREPTOCOCCUS PYOGENES; STREPTOCOCCUS SP. 'GROUP A'; STREPTOCOCCUS SP. 'GROUP B';

EID: 0032873609     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.18.5790-5799.1999     Document Type: Article

References (42)

1. Abouhamad, W. N., and M. D. Manson. 1994. The dipeptide permease of Escherichia coli closely resembles other bacterial transport systems and shows growth-phase-dependent expression. Mol. Microbiol. 14:1077-1092.
2. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl. 1995. Current protocols in molecular biology. John Wiley & Sons, Inc., New York, N.Y.
3. Bailey, J., and C. Manoil. Personal communication.
4. Ballester, S., P. Lopez, J. C. Alonso, M. Espinosa, and S. A. Lacks. 1986. Selective advantage of deletions enhancing chloramphenicol acetyltransferase gene expression in Streptococcus pneumoniae plasmids. Gene 41:153-163.
5. Bardwell, J. C., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589.
6. Berg, P. E. 1981. Cloning and characterization of the Escherichia coli gene coding for alkaline phosphatase. J. Bacteriol. 146:660-667.
7. Bina, J. E., F. Nano, and R. E. Hancock. 1997. Utilization of alkaline phosphatase fusions to identify secreted proteins, including potential efflux proteins and virulence factors from Helicobacter pylori. FEMS Microbiol. Lett. 148:63-68.
8. Brabetz, W., W. Liebl, and K.-H. Schleifer. 1993. Lactose permease of Escherichia coli catalyzes active β-galactoside transport in a gram-positive bacterium. J. Bacteriol. 175:7488-7491.
9. Brickman, E., and J. Beckwith. 1975. Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and ø80 transducing phages. J. Mol. Biol. 96:307-316.
10. Calamia, J., and C. Manoil. 1990. lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion. Proc. Natl. Acad. Sci. USA 87:4937-4941.
11. Chaffin, D. Unpublished observations.
12. Chaffin, D. O., and C. E. Rubens. 1998. Blue/white screening of recombinant plasmids in Gram-positive bacteria by interruption of alkaline phosphatase gene (phoZ) expression. Gene 219:91-99.
13. Cheng, K. J., and J. W. Costerton. 1977. Alkaline phosphatase activity of rumen bacteria. Appl. Environ. Microbiol. 34:586-590.
14. Coleman, J. E., and P. Gettins. 1993. Alkaline phosphatase, solution structure and mechanisms. Adv. Enzymol. Relat. Areas Mol. Biol. 55:381-452.
15. Cruz-Rodz, A. L., and M. S. Gilmore. 1991. Electroporation of glycine-treated Enterococcus faecalis, p. 300. In G. M. Dunny, P. P. Cleary, and L. L. McKay (ed.), Genetics and molecular biology of streptococci, lactococci, and enterococci. American Society for Microbiology, Washington, D.C.
16. Derman, A. I., and J. Beckwith. 1995. Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: a caution for gene fusion studies. J. Bacteriol. 177:3764-3770.
17. Dunny, G., C. Funk, and J. Adsit. 1981. Direct stimulation of the transfer of antibiotic resistance by sex pheromones in Streptococcus faecalis. Plasmid 6:270-278.
18. Engelman, D. M., T. A. Steitz, and A. Goldman. 1986. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15:321-353.
19. Framson, P. E., A. Nittayajarn, J. Merry, P. Youngman, and C. E. Rubens. 1997. New genetic techniques for group B streptococci: high-efficiency transformation, maintenance of temperature-sensitive pWV01 plasmids, and mutagenesis with Tn917. Appl. Environ. Microbiol. 63:3539-3547.
20. Genetics Computer Group. 1999. Wisconsin package, version 9. Genetics Computer Group, Madison, Wis.
21. Hulett, F. M. 1996. The signal-transduction network for Pho regulation in Bacillus subtilis. Mol. Microbiol. 19:933-939.
22. Inouye, H., W. Barnes, and J. Beckwith. 1982. Signal sequence of alkaline phosphatase of Escherichia coli. J. Bacteriol. 149:434-439.
23. Jacks, W. J., Y. Kim, and P. P. Cleary. 1982. Restricted deposition of C3 on M+ group A streptococci: correlation with resistance to phagocytosis. J. Immunol. 128:1897-1902.
24. Kam, W., E. Clauser, Y. S. Kim, Y. W. Kan, and W. J. Rutter. 1985. Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc. Natl. Acad. Sci. USA 82:8715-8719.
25. Kim, E. E., and H. W. Wyckoff. 1991. Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J. Mol. Biol. 218:449-464.
26. Kim, E. E., and H. W. Wyckoff. 1990. Structure of alkaline phosphatases. Clin. Chim. Acta 186:175-187.
27. Lee, E., and C. Manoil. 1994. Mutations eliminating the protein export function of a membrane-spanning sequence. J. Biol. Chem. 269:28822-28828.
28. Lee, M., and C. Manoil. 1996. Molecular genetic analysis of membrane protein topology, p. 189-201. In W. N. Konigs, H. R. Kaback, and J. S. Lolkema (ed.), Transport processes in eukaryotic and prokaryotic organisms. Elsevier Science BV, Amsterdam, The Netherlands.
29. Manoil, C. 1990. Analysis of protein localization by use of gene fusions with complementary properties. J. Bacteriol. 172:1035-1042.
30. Manoil, C., and J. Bailey. 1997. A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease. J. Mol. Biol. 267:250-263.
31. Manoil, C., and J. Beckwith. 1985. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. USA 82:8129-8133
32. Pearce, B. J., Y. B. Yin, and H. R. Masure. 1993. Genetic identification of exported proteins in Streptococcus pneumoniae. Mol. Microbiol. 9:1037-1050.
33. Poquet, I., S. D. Ehrlich, and A. Gruss. 1998. An export-specific reporter designed for gram-positive bacteria: application to Lactococcus lactis. J. Bacteriol. 180:1904-1912.
34. Ross, R. P., and A. Claiborne. 1991. Cloning, sequence and overexpression of NADH peroxidase from Streptococcus faecalis 10Cl. Structural relationship with the flavoprotein disulfide reductases. J. Mol. Biol. 221:857-871.
35. Rubens, C. E., M. R. Wessels, L. M. Heggen, and D. L. Kasper. 1987. Transposon mutagenesis of type III group B streptococcus: correlation of capsule expression with virulence. Proc. Natl. Acad. Sci. USA 84:7208-7212.
36. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
37. Simon, D., and J. J. Ferretti. 1991. Electrotransformation of Streptococcus pyogenes with plasmid and linear DNA. FEMS Microbiol. Lett. 66:219-224.
38. Smith, H., A. de Jong, S. Bron, and G. Venema. 1988. Characterization of signal-sequence-coding regions selected from the Bacillus subtilus chromosome. Gene 70:351-361.
39. Stalhammar-Carlemalm, M., L. Stenberg, and G. Lindahl. 1993. Protein rib: a novel group B streptococcal cell surface protein that confers protective immunity and is expressed by most strains causing invasive infections. J. Exp. Med. 177:1593-1603.
40. Subramaniam, S., R. Unwin, J. Fenton, M. Whitsitt, M. Bhagavan, and A. Stephens. 1999. Biology Workbench 3.0. Computational Biology Group, National Center for Supercomputing Applications, University of Illinois at Urbana-Champaign.
41. Wanner, B. L. 1996. Phosphorus assimilation and control of the phosphate regulon, p. 1357-1381. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Samonella, 2nd ed., vol. 1. ASM Press, Washington, D.C.
42. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.