Heterologous production of Escherichia coli penicillin G acylase in Pseudomonas aeruginosa

Journal of Biotechnology

Volumn 142, Issue 3-4, 2009, Pages 250-258

  Krzeslak, Joanna ^a   Braun, Peter ^a   Voulhoux, Rome ^b   Cool, Robbert H ^a   Quax, Wim J ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b CNRS   (France)

Author keywords

Penicillin G acylase; Propeptide; Pseudomonas; Secretion; Type II pathway

Indexed keywords

PENICILLIN G ACYLASE; PROPEPTIDE; PSEUDOMONAS; SECRETION; TYPE II PATHWAY;

AMINES; BACTERIOLOGY; CELL MEMBRANES; CYTOLOGY; DIFFERENTIAL AMPLIFIERS; ENZYME ACTIVITY; ENZYMES; ESCHERICHIA COLI; MACHINERY; PROGRAMMED CONTROL SYSTEMS; TOXICITY;

DRUG PRODUCTS;

BACTERIAL ENZYME; BETA LACTAMASE; ELASTASE; PENICILLIN AMIDASE; SIGNAL PEPTIDE;

ANIMAL CELL; ARTICLE; BACTERIAL OUTER MEMBRANE; CONTROLLED STUDY; CULTURE MEDIUM; CYTOPLASM; ENZYME ACTIVITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PROTEIN SECRETION; PSEUDOMONAS AERUGINOSA; REPORTER GENE; TEMPERATURE DEPENDENCE;

BACTERIAL PROTEINS; CLONING, MOLECULAR; CYTOPLASM; ESCHERICHIA COLI PROTEINS; MEMBRANE TRANSPORT PROTEINS; PANCREATIC ELASTASE; PENICILLIN AMIDASE; PERIPLASM; PROTEIN SORTING SIGNALS; PROTEIN TRANSPORT; PSEUDOMONAS AERUGINOSA; RECOMBINANT FUSION PROTEINS;

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

EID: 67650113580     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.05.005     Document Type: Article

References (61)

1. Berks B.C. A common export pathway for proteins binding complex redox cofactors?. Mol. Microbiol. 22 (1996) 393-404
2. Berks B.C., Sargent F., and Palmer T. The Tat protein export pathway. Mol. Microbiol. 35 (2000) 260-274
3. Bogsch E., Brink S., and Robinson C. Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein. EMBO J. 16 (1997) 3851-3859
4. Braun P., de Groot A., Bitter W., and Tommassen J. Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa. J. Bacteriol. 180 (1998) 3467-3469
5. Braun P., and Tommassen J. Function of bacterial propeptides. Trends Microbiol. 6 (1998) 6-8
6. Braun P., Tommassen J., and Filloux A. Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa. Mol. Microbiol. 19 (1996) 297-306
7. Brok R., Van Gelder P., Winterhalter M., Ziese U., Koster A.J., de Cock H., Koster M., Tommassen J., and Bitter W. The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity. J. Mol. Biol. 294 (1999) 1169-1179
8. Bruns W., Hoppe J., Tsai H., Bruning H.J., Maywald F., Collins J., and Mayer H. Structure of the penicillin acylase gene from Escherichia coli: a periplasmic enzyme that undergoes multiple proteolytic processing. J. Mol. Appl. Genet. 3 (1985) 36-44
9. Burtscher H., and Schumacher G. Reconstitution in vivo of penicillin G acylase activity from separately expressed subunits. Eur. J. Biochem. 205 (1992) 77-83
10. Chapon V., Czjzek M., El Hassouni M., Py B., Juy M., and Barras F. Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi. J. Mol. Biol. 310 (2001) 1055-1066
11. Choi K.S., Kim J.A., and Kang H.S. Effects of site-directed mutations on processing and activities of penicillin G acylase from Escherichia coli ATCC 11105. J. Bacteriol. 174 (1992) 6270-6276
12. Chou C.P., Yu C.C., Tseng J.H., Lin M.I., and Lin H.K. Genetic manipulation to identify limiting steps and develop strategies for high-level expression of penicillin acylase in Escherichia coli. Biotechnol. Bioeng. 63 (1999) 263-272
13. Cristobal S., de Gier J.W., Nielsen H., and von Heijne G. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18 (1999) 2982-2990
14. Daumy G.O., Danley D., and McColl A.S. Role of protein subunits in Proteus rettgeri penicillin G acylase. J. Bacteriol. 163 (1985) 1279-1281
15. Driessen A.J., Fekkes P., and van der Wolk J.P. The Sec system. Curr. Opin. Microbiol. 1 (1998) 216-222
16. Duggleby H.J., Tolley S.P., Hill C.P., Dodson E.J., Dodson G., and Moody P.C. Penicillin acylase has a single-amino-acid catalytic centre. Nature 373 (1995) 264-268
17. Filloux A., Michel G., and Bally M. GSP-dependent protein secretion in gram-negative bacteria: the Xcp system of Pseudomonas aeruginosa. FEMS Microbiol. Rev. 22 (1998) 177-198
18. Filloux A., Murgier M., Wretlind B., and Lazdunski A. Characterization of two Pseudomonas aeruginosa mutants with defective secretion of extracellular proteins and comparison with other mutants. FEMS Microbiol. Lett. 40 (1987) 159-163
19. Furste J.P., Pansegrau W., Frank R., Blocker H., Scholz P., Bagdasarian M., and Lanka E. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48 (1986) 119-131
20. Genest O., Seduk F., Ilbesr M., Meean V., and Iobbi-Nivol C. Signal peptide protection by specific chaperone. Biochem. Biophys. Res. Commun. 339 (2005) 991-995
21. Haas D., and Holloway B.W. R factor variants with enhanced sex factor activity in Pseudomonas aeruginosa. Mol. Gen. Genet. 144 (1976) 243-251
22. Hirst T.R., Sanchez J., Kaper J.B., Hardy S.J., and Holmgren J. Mechanism of toxin secretion by Vibrio cholerae investigated in strains harboring plasmids that encode heat-labile enterotoxins of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 81 (1984) 7752-7756
23. Ignatova Z., Hornle C., Nurk A., and Kasche V. Unusual signal peptide directs penicillin amidase from Escherichia coli to the Tat translocation machinery. Biochem. Biophys. Res. Commun. 291 (2002) 146-149
24. 2+-binding: implications for folding and maturation of Ntn-hydrolase penicillin amidase from E. coli. J. Mol. Biol. 348 (2005) 999-1014
25. Ize B., Gerard F., Zhang M., Chanal A., Voulhoux R., Palmer T., Filloux A., and Wu L.F. In vivo dissection of the Tat translocation pathway in Escherichia coli. J. Mol. Biol. 317 (2002) 327-335
26. 2+ is a cofactor required for membrane transport and maturation and is a yield-determining factor in high cell density penicillin amidase production. Biotechnol. Prog. 21 (2005) 432-438
27. Keilmann C., Wanner G., and Bock A. Molecular basis of the exclusive low-temperature synthesis of an enzyme in E. coli: penicillin acylase. Biol. Chem. Hoppe Seyler 374 (1993) 983-992
28. Kornacker M.G., and Pugsley A.P. The normally periplasmic enzyme beta-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell-surface enzyme pullulanase. Mol. Microbiol. 4 (1990) 1101-1109
29. Lazdunski A., Guzzo J., Filloux A., Bally M., and Murgier M. Secretion of extracellular proteins by Pseudomonas aeruginosa. Biochimie 72 (1990) 147-156
30. Lindeberg M., Boyd C.M., Keen N.T., and Collmer A. External loops at the C terminus of Erwinia chrysanthemi pectate lyase C are required for species-specific secretion through the out type II pathway. J. Bacteriol. 180 (1998) 1431-1437
31. Lu H.M., and Lory S. A specific targeting domain in mature exotoxin A is required for its extracellular secretion from Pseudomonas aeruginosa. EMBO J. 15 (1996) 429-436
32. McIver K.S., Kessler E., and Ohman D.E. Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities. Microbiology 150 (2004) 3969-3977
33. Merino E., Balbas P., Recillas F., Becerril B., Valle F., and Bolivar F. Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene. Mol. Microbiol. 6 (1992) 2175-2182
34. Muller M., Koch H.G., Beck K., and Schafer U. Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog. Nucleic Acid Res. Mol. Biol. 66 (2001) 107-157
35. Ng D.T., Brown J.D., and Walter P. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134 (1996) 269-278
36. Ohta Y., Hojo H., Aimoto S., Kobayashi T., Zhu X., Jordan F., and Inouye M. Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide [corrected]. Mol. Microbiol. 5 (1991) 1507-1510
37. Pugsley A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57 (1993) 50-108
38. Roa A., and Garcia J.L. New insights into the regulation of the pac gene from Escherichia coli W ATCC 11105. FEMS Microbiol. Lett. 177 (1999) 7-14
39. Sambrook J.F.E.F.a.M.T. Molecular cloning: a laboratory manual (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
40. Santini C.L., Bernadac A., Zhang M., Chanal A., Ize B., Blanco C., and Wu L.F. Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J. Biol. Chem. 276 (2001) 8159-8164
41. Scherrer S., Robas N., Zouheiry H., Branlant G., and Branlant C. Periplasmic aggregation limits the proteolytic maturation of the Escherichia coli penicillin G amidase precursor polypeptide. Appl. Microbiol. Biotechnol. 42 (1994) 85-91
42. Schumacher G., Sizmann D., Haug H., Buckel P., and Bock A. Penicillin acylase from E. coli: unique gene-protein relation. Nucleic Acids Res. 14 (1986) 5713-5727
43. Sio C.F., and Quax W.J. Improved beta-lactam acylases and their use as industrial biocatalysts. Curr. Opin. Biotechnol. 15 (2004) 349-355
44. Slade A., Horrocks A.J., Lindsay C.D., Dunbar B., and Virden R. Site-directed chemical conversion of serine to cysteine in penicillin acylase from Escherichia coli ATCC 11105. Effect on conformation and catalytic activity. Eur. J. Biochem. 197 (1991) 75-80
45. Snyder A., Vasil A.I., Zajdowicz S.L., Wilson Z.R., and Vasil M.L. Role of the Pseudomonas aeruginosa PlcH Tat signal peptide in protein secretion, transcription, and cross-species Tat secretion system compatibility. J. Bacteriol. 188 (2006) 1762-1774
46. Sriubolmas N., Panbangred W., Sriurairatana S., and Meevootisom V. Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase. Appl. Microbiol. Biotechnol. 47 (1997) 373-378
47. Stanley N.R., Sargent F., Buchanan G., Shi J., Stewart V., Palmer T., and Berks B.C. Behaviour of topological marker proteins targeted to the Tat protein transport pathway. Mol. Microbiol. 43 (2002) 1005-1021
48. Thayer M.M., Flaherty K.M., and McKay D.B. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. J. Biol. Chem. 266 (1991) 2864-2871
49. Thomas J.D., Daniel R.A., Errington J., and Robinson C. Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol. Microbiol. 39 (2001) 47-53
50. Valle F., Balbas P., Merino E., and Bolivar F. The role of penicillin amidases in nature and in industry. Trends Biochem. Sci. 16 (1991) 36-40
51. Vandamme E.J., and Voets J.P. Microbial penicillin acylases. Adv. Appl. Microbiol. 17 (1974) 311-369
52. von Heijne G. The signal peptide. J. Membr. Biol. 115 (1990) 195-201
53. von Heijne G. Life and death of a signal peptide. Nature 396 111 (1998) 113
54. Voulhoux R., Ball G., Ize B., Vasil M.L., Lazdunski A., Wu L.F., and Filloux A. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20 (2001) 6735-6741
55. Voulhoux R., Filloux A., and Schalk I.J. Pyoverdine-mediated iron uptake in Pseudomonas aeruginosa: the Tat system is required for PvdN but not for FpvA transport. J. Bacteriol. 188 (2006) 3317-3323
56. Weiner J.H., Bilous P.T., Shaw G.M., Lubitz S.P., Frost L., Thomas G.H., Cole J.A., and Turner R.J. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Cell 93 (1998) 93-101
57. Wetmore D.R., Wong S.L., and Roche R.S. The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus. Mol. Microbiol. 6 (1992) 1593-1604
58. White P.J. The regulation of diaminopimelate decarboxylase activity in Escherichia coli strain w. J. Gen. Microbiol. 96 (1976) 51-62
59. Wong K.R., and Buckley J.T. Site-directed mutagenesis of a single tryptophan near the middle of the channel-forming toxin aerolysin inhibits its transfer across the outer membrane of Aeromonas salmonicida. J. Biol. Chem. 266 (1991) 14451-14456
60. Xu Y., Hsieh M.Y., Narayanan N., Anderson W.A., Scharer J.M., Moo-Young M., and Chou C.P. Cytoplasmic overexpression, folding, and processing of penicillin acylase precursor in Escherichia coli. Biotechnol. Prog. 21 (2005) 1357-1365
61. Yolov A.A., and Shabarova Z.A. Constructing DNA by polymerase recombination. Nucleic Acids Res. 18 (1990) 3983-3986