Heterologous protein secretion in Lactococcus lactis is enhanced by the Bacillus subtilis chaperone-like protein PrsA

Applied Microbiology and Biotechnology

Volumn 73, Issue 4, 2006, Pages 904-914

  Lindholm, Agneta ^a   Ellmén, Ulla ^a,c   Tolonen Martikainen, Marja ^b,d   Palva, Airi ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b FINNISH FOREST RESEARCH INSTITUTE   (Finland)

^c ACADEMY OF FINLAND   (Finland)

^d Finnish Forest Institute   (Finland)

Author keywords

Amylase; Bacillus subtilis; Lactococcus lactis; Penicillinase; Protein secretion; PrsA

Indexed keywords

BACILLUS SUBTILIS; PENICILLINASE; PROTEIN SECRETION;

BACTERIA; GENES; PROTEINS;

BIOTECHNOLOGY;

AMYLASE; BACTERIAL PROTEIN; PENICILLINASE; PROTEIN PRSA; UNCLASSIFIED DRUG;

BACTERIUM; ENZYME ACTIVITY; GENE EXPRESSION; PLASTID; PROTEIN; SECRETION;

AMYQ GENE; ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACILLUS SUBTILIS; BACTERIAL STRAIN; ENZYME ACTIVITY; GENE EXPRESSION; LACTOCOCCUS LACTIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PENP GENE; PLASMID; PROMOTER REGION; PROTEIN PROCESSING; PROTEIN SECRETION; SEQUENCE HOMOLOGY; WESTERN BLOTTING;

ALPHA-AMYLASES; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BLOTTING, WESTERN; LACTOCOCCUS LACTIS; LIPOPROTEINS; MEMBRANE PROTEINS; PENICILLINASE; PLASMIDS; PROTEIN TRANSPORT; RECOMBINANT PROTEINS; TRANSFORMATION, BACTERIAL;

BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS; BACILLUS SUBTILIS; LACTOCOCCUS LACTIS;

EID: 33751508477     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0551-y     Document Type: Article

References (27)

1. Bermudez-Humaran LG, Langella P, Commissaire J, Gilbert S, Le Loir Y, L'Haridon R, Corthier G (2003) Controlled intra- or extracellular production of staphylococcal nuclease and ovine omega interferon in Lactococcus lactis. FEMS Microbiol Lett 224:307-313
2. Bolhuis A, Tjalsma H, Smith HE, de Jong A, Meima R, Venema G, Bron S, van Dijl JM (1999) Evaluation of bottlenecks in the late stages of protein secretion in Bacillus subtilis. Appl Environ Microbiol 65:2934-2941
3. Bonifacino JS, Dell'Angelica EC, Springer TA (eds) (1999) Analysis of proteins. Immunoprecipitation. Green Publishing Associates, New York, pp 10.16.1-10.16.29
4. Colomer-Pallas A, Petit-Glatron MF, Chambert R (2004) Bacillus subtilis alpha-amylase: interactions of a partially folded conformer with small unilamellar vesicles. Biochim Biophys Acta 1660:16-23
5. de Ruyter PG, Kuipers OP, Beerthuyzen MM, van Alen-Boerrigter I, de Vos WM (1996a) Functional analysis of promoters in the nisin gene cluster of Lactococcus lactis. J Bacteriol 178:3434-3439
6. de Ruyter PG, Kuipers OP, de Vos WM (1996b) Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol 62:3662-3667
7. Drouault S, Anba J, Bonneau S, Bolotin A, Ehrlich SD, Renault P (2002) The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis. Appl Environ Microbiol 68:3932-3942
8. Holo H, Nes IF (1995) Transformation of Lactococcus by electroporation. Methods Mol Biol 47:195-199
9. Kontinen VP, Sarvas M (1988) Mutants of Bacillus subtilis defective in protein export. J Gen Microbiol 134:2333-2344
10. Kontinen VP, Sarvas M (1993) The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion. Mol Microbiol 8:727-737
11. Kontinen VP, Saris P, Sarvas M (1991) A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export. Mol Microbiol 5:1273-1283
12. Le Loir Y, Azevedo V, Oliveira SC, Freitas DA, Miyoshi A, Bermudez-Humaran LG, Nouaille S, Ribeiro LA, Leclercq S, Gabriel JE, Guimaraes VD, Oliveira MN, Charlier C, Gautier M, Langella P (2005) Protein secretion in Lactococcus lactis: an efficient way to increase the overall heterologous protein production. Microb Cell Fact 4:2
13. Leskela S, Wahlstrom E, Kontinen VP, Sarvas M (1999) Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: characterization of the lgt gene. Mol Microbiol 31:1075-1085
14. Lindholm A, Smeds A, Palva A (2004) Receptor binding domain of Escherichia coli F18 fimbrial adhesin FedF can be both efficiently secreted and surface displayed in a functional form in Lactococcus lactis. Appl Environ Microbiol 70:2061-2071
15. Neugebauer K, Sprengel R, Schaller H (1981) Penicillinase from Bacillus licheniformis: nucleotide sequence of the gene and implications for the biosynthesis of a secretory protein in a gram-positive bacterium. Nucleic Acids Res 9:2577-2588
16. Novotny R, Scheberl A, Giry-Laterriere M, Messner P, Schaffer C (2005) Gene cloning, functional expression and secretion of the S-layer protein SgsE from Geobacillus stearothermophilus NRS 2004/3a in Lactococcus lactis. FEMS Microbiol Lett 242:27-35
17. Otto R, Brink Bt, Veldkamp H, Konings WN (1983) The relation between growth rate and electrochemical proton gradient of Streptococcus cremoris. FEMS Microbiol Lett 16:69-74
18. Palva I (1982) Molecular cloning of alpha-amylase gene from Bacillus amyloliquefaciens and its expression in B. subtilis. Gene 19:81-87
19. Poolman B, Konings WN (1988) Relation of growth of Streptococcus lactis and Streptococcus cremoris to amino acid transport. J Bacteriol 170:700-707
20. Sarvas M, Harwood CR, Bron S, van Dijl JM (2004) Post-translocational folding of secretory proteins in gram-positive bacteria. Biochim Biophys Acta 1694:311-327
21. Savijoki K, Kahala M, Palva A (1997) High level heterologous protein production in Lactococcus and Lactobacillus using a new secretion system based on the Lactobacillus brevis S-layer signals. Gene 186:255-262
22. Simon D, Chopin A (1988) Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie 70:559-566
23. Simons K, Sarvas M, Garoff H, Helenius A (1978) Membrane-bound and secreted forms of penicillinase from Bacillus licheniformis. J Mol Biol 126:673-690
24. Takkinen K, Pettersson RF, Kalkkinen N, Palva I, Soderlund H, Kaariainen L (1983) Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene. J Biol Chem 258:1007-1013
25. Vitikainen M, Pummi T, Airaksinen U, Wahlstrom E, Wu H, Sarvas M, Kontinen VP (2001) Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis. J Bacteriol 183:1881-1890
26. Vitikainen M, Hyyrylainen HL, Kivimaki A, Kontinen VP, Sarvas M (2005) Secretion of heterologous proteins in Bacillus subtilis can be improved by engineering cell components affecting posttranslocational protein folding and degradation. J Appl Microbiol 99:363-375
27. Wahlstrom E, Vitikainen M, Kontinen VP, Sarvas M (2003) The extracytoplasmic folding factor PrsA is required for protein secretion only in the presence of the cell wall in Bacillus subtilis. Microbiology 149:569-577