Preparation and biophysical characterization of recombinant Pseudomonas aeruginosa phosphorylcholine phosphatase

Protein Expression and Purification

Volumn 71, Issue 2, 2010, Pages 153-159

  Beassoni, Paola R ^a   Berti, Federico Pérez de ^b   Otero, Lisandro H ^a   Risso, Valeria A ^b,c   Ferreyra, Raul G ^b,c   Lisa, Angela T ^a   Domenech, Carlos E ^a   Ermácora, Mario R ^b,c  

^a DEPARTAMENTO DE QUÍMICA   (Argentina)

^b UNIVERSIDAD NACIONAL DE QUILMES   (Argentina)

^c Facultad de Ciencias Naturales e Instituto M Lillo   (Argentina)

Author keywords

Circular dichroism; Fluorescence; Metal binding; Phosphorylcholine phosphatase; Protein folding; Pseudomonas aeruginosa

Indexed keywords

PHOSPHATASE; PHOSPHORYLCHOLINE;

ARTICLE; BIOPHYSICS; CATALYSIS; CELL INCLUSION; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS INFECTION;

BIOPHYSICAL PHENOMENA; CATALYSIS; ESCHERICHIA COLI; INCLUSION BODIES; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLCHOLINE; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS INFECTIONS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 77949654439     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.01.006     Document Type: Article

References (35)

1. Bodey G.P., Bolivar R., Fainstein V., and Jadeja L. Infections caused by Pseudomonas aeruginosa. Rev. Infect. Dis. 5 (1983) 279-313
2. Lyczak J.B., Cannon C.L., and Pier G.B. Establishment of Pseudomonas aeruginosa infection: lessons from a versatile opportunist. Microb. Infect. 2 (2000) 1051-1060
3. Doring G., Horz M., Ortelt J., Grupp H., and Wolz C. Molecular epidemiology of Pseudomonas aeruginosa in an intensive care unit. Epidemiol. Infect. 110 (1993) 427-436
4. Govan J.R., and Deretic V. Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiol. Rev. 60 (1996) 539-574
5. S.K. Fridkin, R.P. Gaynes, Antimicrobial resistance in intensive care units, Clin. Chest. Med. 20 (1999) 303-316 (viii).
6. Hancock R.E., and Speert D.P. Antibiotic resistance in Pseudomonas aeruginosa: mechanisms and impact on treatment. Drug Resist. Updat. 3 (2000) 247-255
7. Lisa A.T., Lucchesi G.I., and Domenech C.E. Pathogenicity of Pseudomonas aeruginosa and its relationship to the choline metabolism through the action of cholinesterase, acid phosphatase, and phospholipase C. Curr. Microbiol. 29 (1994) 193-199
8. Lisa A.T., Casale C.H., and Domenech C.E. Cholinesterase, acid phosphatase, and phospholipase C of Pseudomonas aeruginosa under hyperosmotic conditions in a high-phosphate medium. Curr. Microbiol. 28 (1994) 71-76
9. Casale C.H., Lisa A.T., Lucchesi G.I., and Domenech C.E. The production of labeled betaine by incubation of osmolyte-free Pseudomonas aeruginosa with radioactive choline. Curr. Microbiol. 29 (1994) 295-299
10. Lucchesi G.I., Lisa T.A., Casale C.H., and Domenech C.E. Carnitine resembles choline in the induction of cholinesterase, acid phosphatase, and phospholipase C and in its action as an osmoprotectant in Pseudomonas aeruginosa. Curr. Microbiol. 30 (1995) 55-60
11. Kilbourn J.P. Bacterial content and ionic composition of sputum in cystic fibrosis. Lancet 1 (1978) 334
12. Lisa A.T., Beassoni P.R., Massimelli M.J., Otero L.H., and Domenech C.E. In: Mendez-Vilas A. (Ed). Communicating Current Research and Educational Topics and Trends in Applied Microbiology (2007), Formatex Research Center, Badajoz, Spain 255-262
13. Salvano M.A., and Domenech C.E. Kinetic properties of purified Pseudomonas aeruginosa phosphorylcholine phosphatase indicated that this enzyme may be utilized by the bacteria to colonize in different environments. Curr. Microbiol. 39 (1999) 1-8
14. Massimelli M.J., Beassoni P.R., Forrellad M.A., Barra J.L., Garrido M.N., Domenech C.E., and Lisa A.T. Identification, cloning, and expression of Pseudomonas aeruginosa phosphorylcholine phosphatase gene. Curr. Microbiol. 50 (2005) 251-256
15. Beassoni P.R., Otero L.H., Massimelli M.J., Lisa A.T., and Domenech C.E. Critical active-site residues identified by site-directed mutagenesis in Pseudomonas aeruginosa phosphorylcholine phosphatase, a new member of the haloacid dehalogenases hydrolase superfamily. Curr. Microbiol. 53 (2006) 534-539
16. Beassoni P.R., Otero L.H., Lisa A.T., and Domenech C.E. Using a molecular model and kinetic experiments in the presence of divalent cations to study the active site and catalysis of Pseudomonas aeruginosa phosphorylcholine phosphatase. Biochim. Biophys. Acta 1784 (2008) 2038-2044
17. Riddles P.W., Blakeley R.L., and Zerner B. Reassessment of Ellman's reagent. Methods Enzymol. 91 (1983) 49-60
18. Silverstein R.M. The determination of the molar extinction coefficient of reduced DTNB. Anal. Biochem. 63 (1975) 281-282
19. Fersht A. Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding (1999), Freeman, New York
20. Clerico E.M., and Ermácora M.R. Tryptophan mutants of intestinal fatty acid-binding protein: ultraviolet absorption and circular dichroism studies. Arch. Biochem. Biophys. 395 (2001) 215-224
21. Savitzky A., and Golay M.J.E. Smoothing and differentiation of data by simplified least squares procedures. Anal. Chem. 36 (1964) 1627-1639
22. Santos J., Gebhard L.G., Risso V.A., Ferreyra R.G., Rossi J.P., and Ermácora M.R. Folding of an abridged beta-lactamase. Biochemistry 43 (2004) 1715-1723
23. Frate M.C., Lietz E.J., Santos J., Rossi J.P., Fink A.L., and Ermácora M.R. Export and folding of signal-sequenceless Bacillus licheniformis beta-lactamase in Escherichia coli. Eur. J. Biochem. 267 (2000) 3836-3847
24. Chauhan U.P., and Sarkar B.C. Use of calmagite for the determination of traces of magnesium in biological materials. Anal. Biochem. 32 (1969) 70-80
25. Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340 (2004) 783-795
26. von Heijne G. Signal sequences. The limits of variation. J. Mol. Biol. 184 (1985) 99-105
27. von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341 (1989) 456-458
28. Lewenza S., Gardy J.L., Brinkman F.S., and Hancock R.E. Genome-wide identification of Pseudomonas aeruginosa exported proteins using a consensus computational strategy combined with a laboratory-based PhoA fusion screen. Genome Res. 15 (2005) 321-329
29. Bowden G.A., and Georgiou G. Folding and aggregation of beta-lactamase in the periplasmic space of Escherichia coli. J. Biol. Chem. 265 (1990) 16760-16766
30. Nozaki Y. Determination of tryptophan, tyrosine, and phenylalanine by second derivative spectrophotometry. Arch. Biochem. Biophys. 277 (1990) 324-333
31. Deleage G., and Geourjon C. An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput. Appl. Biosci. 9 (1993) 197-199
32. Domenech C.E., Lisa T.A., Salvano M.A., and Garrido M.N. Pseudomonas aeruginosa acid phosphatase. Activation by divalent cations and inhibition by aluminium ion. FEBS Lett. 299 (1992) 96-98
33. Cronin A., Homburg S., Durk H., Richter I., Adamska M., Frere F., and Arand M. Insights into the catalytic mechanism of human sEH phosphatase by site-directed mutagenesis and LC-MS/MS analysis. J. Mol. Biol. 383 (2008) 627-640
34. Wang W., Cho H.S., Kim R., Jancarik J., Yokota H., Nguyen H.H., Grigoriev I.V., Wemmer D.E., and Kim S.H. Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states. J. Mol. Biol. 319 (2002) 421-431
35. Strickland E.H. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 2 (1974) 113-175