Identification and functional characterisation of cellobiose and lactose transport systems in Lactococcus lactis IL1403

The following observations showed that 2-deoxy-D-galactose is a useful tool for the isolation and elucidation of the activity of one system for galactose uptake into Escherichia coli. 1. 2-Deoxygalactose, which is not a substrate for growth of E. coli, was transported into strains of the organism induced for galactose transport. 2. By using appropriate mutants it was shown that 2-deoxygalactose is a much better substrate for the galactose-transport system than for the methyl galactoside-transport system. This was confirmed by the results of mutual inhibition studies with substrates of each transport system. 3. The glucose-, arabinose- or lactose-transport systems did not effect significant transport of 2-deoxygalactose. 4. Like other substrates of the galactose-transport system, 2-deoxygalactose promoted effective proton uptake into de-energized suspensions of appropriate E. coli strains. 5. The S183 series of E. coli mutants were found to contain a constitutive galactose-transport system, if 2-deoxygalactose transport is used as one criterion for such activity.

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Alternative Lactose Catabolic Pathway in Lactococcus lactis IL1403

Applied and Environmental Microbiology ◽

10.1128/aem.71.10.6060-6069.2005 ◽

2005 ◽

Vol 71 (10) ◽

pp. 6060-6069 ◽

Cited By ~ 26

Author(s):

Tamara Aleksandrzak-Piekarczyk ◽

Jan Kok ◽

Pierre Renault ◽

Jacek Bardowski

Keyword(s):

Lactococcus Lactis ◽

Protein A ◽

Lactose Hydrolysis ◽

Galactosidase Activity ◽

Solid Media ◽

Pathway Gene ◽

Leloir Pathway ◽

Catabolite Control Protein A ◽

Lactis Il1403 ◽

Strong Control

ABSTRACT In this study, we present a glimpse of the diversity of Lactococcus lactis subsp. lactis IL1403 β-galactosidase phenotype-negative mutants isolated by negative selection on solid media containing cellobiose or lactose and X-Gal (5-bromo-4-chloro-3-indolyl-β-d-galactopyranoside), and we identify several genes essential for lactose assimilation. Among these are ccpA (encoding catabolite control protein A), bglS (encoding phospho-β-glucosidase), and several genes from the Leloir pathway gene cluster encoding proteins presumably essential for lactose metabolism. The functions of these genes were demonstrated by their disruption and testing of the growth of resultant mutants in lactose-containing media. By examining the ccpA and bglS mutants for phospho-β-galactosidase activity, we showed that expression of bglS is not under strong control of CcpA. Moreover, this analysis revealed that although BglS is homologous to a putative phospho-β-glucosidase, it also exhibits phospho-β-galactosidase activity and is the major enzyme in L. lactis IL1403 involved in lactose hydrolysis.

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Starvation-Induced Stress Resistance in Lactococcus lactis subsp. lactis IL1403

Applied and Environmental Microbiology ◽

10.1128/aem.60.9.3474-3478.1994 ◽

1994 ◽

Vol 60 (9) ◽

pp. 3474-3478 ◽

Cited By ~ 79

Author(s):

Axel Hartke ◽

Sandrine Bouche ◽

Xavier Gansel ◽

Philippe Boutibonnes ◽

Yanick Auffray

Keyword(s):

Lactococcus Lactis ◽

Stress Resistance ◽

Lactococcus Lactis Subsp ◽

Induced Stress ◽

Lactis Il1403

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Low-redundancy sequencing of the entire Lactococcus lactis IL1403 genome

Lactic Acid Bacteria: Genetics, Metabolism and Applications ◽

10.1007/978-94-017-2027-4_2 ◽

1999 ◽

pp. 27-76 ◽

Cited By ~ 4

Author(s):

Alexander Bolotin ◽

Stéphane Mauger ◽

Karine Malarme ◽

S. Dusko Ehrlich ◽

Alexei Sorokin

Keyword(s):

Lactococcus Lactis ◽

Lactis Il1403

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Chimeras of Mature Pediocin PA-1 Fused to the Signal Peptide of Enterocin P Permits the Cloning, Production, and Expression of Pediocin PA-1 in Lactococcus lactis

Journal of Food Protection ◽

10.4315/0362-028x-70.12.2792 ◽

2007 ◽

Vol 70 (12) ◽

pp. 2792-2798 ◽

Cited By ~ 16

Author(s):

MARÍA MARTÍN ◽

JORGE GUTIÉRREZ ◽

RAQUEL CRIADO ◽

CARMEN HERRANZ ◽

LUIS M. CINTAS ◽

...

Keyword(s):

Antimicrobial Activity ◽

Lactococcus Lactis ◽

Signal Peptide ◽

Biologically Active ◽

Enzyme Linked Immunosorbent Assay ◽

Minimum Requirement ◽

Recombinant Plasmids ◽

Genes Encoding ◽

Lactis Il1403 ◽

Enterocin P

Chimeras of pediocin PA-1 (PedA-1), a bacteriocin produced by Pediococcus acidilactici PLBH9, fused to the signal peptide of enterocin P (EntP), a sec-dependent bacteriocin produced by Enterococcus faecium P13, permitted the production of PedA-1 in Lactococcus lactis. Chimeric genes encoding the EntP signal peptide (SPentP) fused to mature PedA-1 (pedA), with or without its immunity gene (pedB), were cloned into the expression vector pMG36c to generate the recombinant plasmids pMPP9 (SPentP:pedA) and pMPP14i (SPentP:pedA+pedB). Transformation of competent L. lactis subsp. lactis IL1403, L. lactis subsp. cremoris NZ9000, and L. lactis subsp. lactis DPC5598 with the recombinant plasmids has permitted the detection and quantitation of PedA-1 and the coproduction of nisin A and PedA-1 in supernatants of producer cells with specific anti–PedA-1 antibodies and a noncompetitive indirect enzyme-linked immunosorbent assay. Recombinant L. lactis hosts carrying pMPP9 or pMPP14i displayed antimicrobial activity, suggesting that mature PedA-1 fused to SPEntP is the minimum requirement for the synthesis, processing, and secretion of biologically active PedA-1 in L. lactis. However, the production and antimicrobial activity of the PedA-1 produced by L. lactis was lower than that produced by the P. acidilactici control strains.

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