Cloning of a
            <i>Streptococcus lactis</i>
            subsp.
            <i>lactis</i>
            Chromosomal Fragment Associated with the Ability To Grow in Milk

Tynkkynen, Soile; Suominen, M.

doi:10.1128/aem.53.7.1584-1588.1987

Cited by 52 publications

(14 citation statements)

References 17 publications

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“…The oligopeptide transport system is the main system involved in the acquisition of nutrients from casein in milk by L. lactis Tynkkynen et al 1993;Kunji et al 1998). Mutant strains of L. lactis lacking a functional Opp are unable to grow in milk (von Wright et al 1987;Tynkkynen et al 1993) and accumulate amino acids internally (Kunji et al 1995). AJK002.1 achieved final bacterial cell counts in milk of between 1% and 10% that of the wildtype strain, but exhibited a similar rate of growth to the parent strain for up to 12 h. Hence, although peptide utilization in this strain had been altered, this appeared to have a yield-limiting, rather than a rate-limiting effect on growth of Strep.…”

Section: Discussionmentioning

confidence: 99%

“…The acquisition of nitrogenous nutrients from milk by Lactococcus lactis requires an intact oligopeptide transport system (Kunji et al , 1998Tynkkynen et al 1993). Mutant strains of L. lactis lacking such a system were unable to grow in milk (von Wright et al 1987;Tynkkynen et al 1993) and accumulate amino acids internally (Kunji et al 1995). During intramammary infection, Strep.…”

Section: Introductionmentioning

confidence: 99%

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Isolation and characterization of a mutant strain of Streptococcus uberis, which fails to utilize a plasmin derived β-casein peptide for the acquisition of methionine

Smith

Kitt

Ward

et al. 2002

Journal of Applied Microbiology

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Aims: To isolate and characterize a mutant of Streptococcus uberis strain 0140J which fails to utilize a plasmin derived β‐casein peptide for the acquisition of methionine.  Methods and Results: Random insertional mutagenesis was used to isolate a mutant strain of Strep. uberis 0140J which was unable to utilize methionine from within a casein‐derived peptide. The altered gene in the mutant strain showed homology to an oligopeptide permease gene of Streptococcus pyogenes (oppF). The mutant was unable to obtain specific amino acids from defined peptides of various lengths and its growth yield in skimmed milk was between 1 and 10% that of the wild‐type strain, but was restored following the inclusion of these amino acids.  Conclusions: The oligopeptide permease homologue of Strep. uberis 0140J is necessary for the utilization of amino acids from within specific peptides. Efficient acquisition of essential amino acids by Strep. uberis 0140J is required for the bacterium to achieve an optimum yield in milk.  Significance and Impact of the Study:Streptococcus uberis is a major agent of bovine mastitis with a corresponding high economic loss. By targeting metabolic pathways essential to the growth of Strep. uberis it may be possible to prevent the establishment of growth of the bacterium in milk. This study has identified the acquisition of essential amino acids as playing a role in the growth of Strep. uberis in milk.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of a mutant strain of Streptococcus uberis, which fails to utilize a plasmin derived β-casein peptide for the acquisition of methionine

Smith

Kitt

Ward

et al. 2002

Journal of Applied Microbiology

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“…Overnight cultures of strains Wicky and STG1 were diluted 106 in THmedium. Then 0.5 m g ml 7 1 of plasmid pVS2 (chloramphenicol resistant) was added (von Wright et al, 1987), and each sample was treated with 200 ng ml 7 1 of synthetic CSP1 or CSP2. Control samples received no competence pheromone.…”

Section: Methodsmentioning

confidence: 99%

Identification of the streptococcal competence‐pheromone receptor

Håvarstein

Gaustad²,

Nes

et al. 1996

Molecular Microbiology

271

233

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Competence for genetic transformation in certain species of streptococci has been known for many years to be induced by a secreted protease-sensitive pheromone, referred to as the competence factor or activator, which acts as a quorum-sensing signal to co-ordinate expression of late competence genes. We recently reported identification of the pheromone of Streptococcus pneumoniae strain Rx as a small unmodified peptide, which was termed competence-stimulating peptide (CSP). By identifying the gene (comC) encoding the Rx CSP we were able to show that it is synthesized as a precursor peptide containing an N-terminal double-glycine type leader. In the present work, we describe two alleles of the corresponding gene from Streptococcus gordonii strains Challis and NCTC 7865, which are strains with distinct competence pheromones and corresponding specific pheromone reactivities. In addition, the nucleic acid sequences of two genes located downstream of comC were determined; interestingly, these genes encode a two-component signal transduction system. We therefore speculated that their products, a histidine kinase (ComD) and its cognate response regulator (ComE), act downstream of the CSP in competence regulation. By tracing the CSP specificity of the competence response in these strains to strain-specific alleles of comD, we obtained evidence demonstrating that the histidine kinase ComD is the competence-pheromone receptor.

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“…The 5 kb Hindlll restriction fragment which harbours the complete plnABCD operon (Diep et aL, 1994) was ligated into pVS2 vector (von Wright et aL, 1987) at its unique Hindlll site. The recombinant plasmid (pVH52) was transformed into L. sake Lb706B, as described by Axelsson et aL (1993).…”

Section: Heterologous Expression Of the Induction Factor/plantaricin Amentioning

confidence: 99%

A bacteriocin‐like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11

Diep

H»varstein

Nes

1995

Molecular Microbiology

165

143

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In this study, we show that bacteriocin production in Lactobacillus plantarum C11 is an inducible process triggered by a secreted protein factor produced by the bacteriocin producer itself. The induction factor was identified to be plantaricin A, a bacteriocin-like peptide whose gene (plnA) is located in the same operon as a two-component regulatory system (plnBCD). When L. plantarum C11 cultures were depleted for plantaricin A, either by growing individual colonies on agar plates or by starting a new culture with a highly diluted inoculum, no bacteriocin was produced during the following growth. When chemically synthesized plantaricin A or purified bacterially produced plantaricin A was added to non-producing cultures, bacteriocin production was induced. Only 1 ng ml-1 plantaricin A is sufficient to induce the bacteriocin production in non-producing L. plantarum C11, and bacteriocin activity appears in the growth medium approximately 150 min after induction. Northern analyses, using a plnA-specific probe, demonstrated that plantaricin A is able to induce its own synthesis by transcription of the plnABCD operon, and this is observed approximately 15 min after adding plantaricin A. Furthermore, heterologous expression of the plnABCD operon in a Lactobacillus sake strain showed that the conditioned growth medium contained the active induction factor. Neither synthetic nor expressed plantaricin A from the heterologous system possesses any bacteriocin activity, suggesting that plantaricin A is primarily an induction factor and not a bacteriocin as claimed earlier.

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Cloning of a Streptococcus lactis subsp. lactis Chromosomal Fragment Associated with the Ability To Grow in Milk

Cited by 52 publications

References 17 publications

Isolation and characterization of a mutant strain of Streptococcus uberis, which fails to utilize a plasmin derived β-casein peptide for the acquisition of methionine

Isolation and characterization of a mutant strain of Streptococcus uberis, which fails to utilize a plasmin derived β-casein peptide for the acquisition of methionine

Identification of the streptococcal competence‐pheromone receptor

A bacteriocin‐like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11

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