Reconstruction of the proteolytic pathway for use of β-casein by Lactococcus lactis

Molecular Microbiology

Volumn 27, Issue 6, 1998, Pages 1107-1118

  Kunji, Edmund R S ^a   Fang, Gang ^a   Jeronimus Stratingh, C Margot ^a   Bruins, Andries P ^a   Poolman, Bert ^a   Konings, Wil N ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BETA CASEIN; MUTANT PROTEIN; PROTEINASE;

AMINO ACID SYNTHESIS; ARTICLE; BACTERIAL CELL WALL; ENZYME SPECIFICITY; ENZYME SUBSTRATE; LACTOCOCCUS LACTIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TRANSPORT;

AMINO ACID SEQUENCE; AMINO ACIDS; BACTERIAL PROTEINS; CARRIER PROTEINS; CASEINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ENDOPEPTIDASES; EXTRACELLULAR SPACE; KINETICS; LACTOCOCCUS LACTIS; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE FRAGMENTS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

EID: 0031883012     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00769.x     Document Type: Article

References (20)

1. Anderson, D.G., and McKay, L.L. (1983) Simple and rapid method for isolating large plasmid DNA from lactic streptococci. Appl Environ Microbiol 46: 549-552.
2. Bruins, A.P., Covey, T.R., and Henion, J.D. (1987) Ion spray interface for combined liquid chromatography/atmospheric pressure ionization mass spectrometry. Anal Chem 59: 2642-2646.
3. Bruins, A.P., and Beaugrand, C. (1988) LC/MS with atmospheric pressure ionization using the Nermag R-30-10 triple quadrupole mass spectrometer. In Proceedings of the 36th ASMS Conference on Mass Spectrometry and Allied Topics, San Francisco, CA. pp. 1241-1242.
4. Buist, G., Kok, J., Leenhouts, K.J., Dabrowska, M., Venema, G., and Haandrikman, A.J. (1995) Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J Bacteriol 177: 1554-1563.
5. Buist, G., Kasens, H., Nauta, A., van Sinderen, D., Venema, G., and Kok, J. (1997) Autolysis of Lactococcus lactis caused by induced overproduction of its major autolysin AcmA. Appl Environ Microbiol 63: 2722-2728.
6. Gasson, M.J. (1983) Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J Bacteriol 154: 1-9.
7. Holo, H., and Nes, I.F. (1989) High-frequency transformation, by electroporation, of Lactococcus lactis ssp. cremoris grown with glycine in osmotically stabilized media. Appl Environ Microbiol 55: 3119-3123.
8. Holt, C., and Sawyer, L. (1988) Primary and predicted secondary structures of caseins in relation to their biological functions. Prot Engineer 2: 251-259.
9. I-type proteinase of Lactococcus lactis hydrolyses β-casein into more than one hundred different oligopeptides. J Bacteriol 177: 3472-3478.
10. Katta, V., Chowdhury, S. K., and Chait, B. T. (1991) Use of a single-quadrupole mass spectrometer for collision-induced dissociation studies of multiply charged peptide ions produced by electrospray ionization. Anal Chem 63: 174-178.
11. Kunji, E.R.S., Smid, E.J., Plapp, R., Poolman, B., and Konings, W.N. (1993) Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis. J Bacteriol 175: 2052-2059.
12. Kunji, E.R.S., Hagting, A., de Vries, C.J., Juillard, V., Haandrikman, A.J., Poolman, B., and Konings, W.N. (1995) Transport of β-casein-derived peptides by the oligopeptide transport system is a crucial step in the proteolytic pathway of Lactococcus lactis. J Biol Chem 270: 1569-1574.
13. Kunji, E. R. S., Mierau, I., Hagting, A., Poolman, B., and Konings, W. N. (1996a) The proteolytic systems of lactic acid bacteria. Antonie van Leeuwenhoek 70: 187-221.
14. Kunji, E.R.S., Mierau, I., Poolman, B., Kok, J., Konings, W.N., and Venema, G. (1996b) The fate of peptides in peptidase deficient mutants of Lactococcus lactis. Mol Microbiol 21: 123-131.
15. Lee, T.D., and Vemuri, S. (1990) MacProMass: a computer program to correlate mass spectral data to peptide and protein structures. Biomed Environ Mass Spectrom 19: 639-645.
16. Lowry, O.H., Rosebrough, N.J., Farr, A.J., and Randall, R.J. (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193: 265-275.
17. Mierau, I., Kunji, E.R.S., Leenhouts, K., Poolman, B., Kok, J., Konings, W.N., and Venema, G. (1996) Multiple peptidase-deficient mutants of Lactococcus lactis are severely impaired in their ability to growth in milk. J Bacteriol 178: 2794-2803.
18. Roepstorff, P., and Fohlman, J. (1984) Proposal for a common nomenclature for the sequence ions in mass spectra of peptides. Biomed Mass Spectrom 11: 601.
19. Tame, J.R.H., Murshudow, G.N., Dodson, E.J., Neil, T.K., Dodson, G.G., Higgins, C.F., and Wilkinson, A.J. (1994) The structural basis of sequence-independent peptide binding by OppA protein. Science 264: 1578-1581.
20. Tynkkynen, S., Buist, G., Kunji, E., Kok, J., Poolman, B., Venema, G., and Haandrikman, A.J. (1993) Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis. J Bacteriol 175: 7523-7532.