scholarly journals Nisin-Controlled Production of Pediocin PA-1 and Colicin V in Nisin- and Non-Nisin-Producing Lactococcus lactis Strains

2004 ◽  
Vol 70 (8) ◽  
pp. 5030-5032 ◽  
Author(s):  
Nikki Horn ◽  
Antonio Fernández ◽  
Helen M. Dodd ◽  
Michael J. Gasson ◽  
Juan M. Rodríguez
Keyword(s):  
Lactococcus Lactis ◽  
Chimeric Genes ◽  
Two Component ◽  
Genes Encoding ◽  
Colicin V ◽  
Nisin Producer

ABSTRACT The introduction of chimeric genes encoding the fusion leader of lactococcin A-propediocin PA-1 or procolicin V under the control of the inducible nisA promoter and the lactococcin A-dedicated secretion genes (lcnCD) into Lactococcus lactis strains, including a nisin producer, expressing the two component regulator NisRK led to the production or pediocin PA-1 or colicin V, respectively.

scholarly journals Intra- and Interspecies Signaling betweenStreptococcus salivarius and Streptococcus pyogenes Mediated by SalA and SalA1 Lantibiotic Peptides

2001 ◽  
Vol 183 (13) ◽  
pp. 3931-3938 ◽  
Author(s):  
M. Upton ◽  
J. R. Tagg ◽  
P. Wescombe ◽  
H. F. Jenkinson
Keyword(s):  
Streptococcus Pyogenes ◽  
Response Regulator ◽  
Genetic Locus ◽  
Two Component System ◽  
Peptide Modification ◽  
Insertional Inactivation ◽  
Two Component ◽  
Genes Encoding ◽  
Dose Dependent

ABSTRACT Streptococcus salivarius 20P3 produces a 22-amino-acid residue lantibiotic, designated salivaricin A (SalA), that inhibits the growth of a range of streptococci, including all strains ofStreptococcus pyogenes. Lantibiotic production is associated with the sal genetic locus comprisingsalA, the lantibiotic structural gene; salBCTXgenes encoding peptide modification and export machinery proteins; andsalYKR genes encoding a putative immunity protein and two-component sensor-regulator system. Insertional inactivation ofsalB in S. salivarius 20P3 resulted in abrogation of SalA peptide production, of immunity to SalA, and ofsalA transcription. Addition of exogenous SalA peptide tosalB mutant cultures induced dose-dependent expression ofsalA mRNA (0.2 kb), demonstrating that SalA production was normally autoregulated. Inactivation of salR encoding the response regulator of the SalKR two-component system led to reduced production of, and immunity to, SalA. The sal genetic locus was also present in S. pyogenes SF370 (M type 1), but because of a deletion across the salBCT genes, the corresponding lantibiotic peptide, designated SalA1, was not produced. However, in S. pyogenes T11 (M type 4) the sallocus gene complement was apparently complete, and active SalA1 peptide was synthesized. Exogenously added SalA1 peptide from S. pyogenes T11 induced salA1 transcription in S. pyogenes SF370 and in an isogenic S. pyogenes T11salB mutant and salA transcription in S. salivarius 20P3 salB. Thus, SalA and SalA1 are examples of streptococcal lantibiotics whose production is autoregulated. These peptides act as intra- and interspecies signaling molecules, modulating lantibiotic production and possibly influencing streptococcal population ecology in the oral cavity.

scholarly journals Putative VanRS-Like Two-Component Regulatory System Associated with the Inducible Glycopeptide Resistance Cluster of Paenibacillus popilliae

2005 ◽  
Vol 49 (7) ◽  
pp. 2625-2633 ◽  
Author(s):  
Henry Fraimow ◽  
Christopher Knob ◽  
Inmaculada A. Herrero ◽  
Robin Patel
Keyword(s):  
Regulatory System ◽  
Growth Curves ◽  
Upstream Region ◽  
Bacillus Halodurans ◽  
Human Pathogens ◽  
Glycopeptide Resistance ◽  
Transposase Gene ◽  
Two Component ◽  
Genes Encoding ◽  
Paenibacillus Lentimorbus

ABSTRACT Paenibacillus popilliae contains vanF encoding a putative d-Ala:d-lactate (d-Lac) ligase, VanF, as part of the vanY F Z F H F FX F cluster that is similar in structure to the enterococcal vanA and vanB clusters. Using growth curves, we demonstrated that vancomycin resistance in P. popilliae is inducible. Using degenerate oligonucleotides targeted at bacterial cell wall ligases, we identified a second ligase gene with features of a d-Ala:d-Ala ligase in both P. popilliae and the related, vancomycin-susceptible, Paenibacillus lentimorbus. The 3,380-bp region upstream of vanY F Z F H F FX F in P. popilliae ATCC 14706 was sequenced and found to contain genes encoding a putative two-component regulator, VanRFSF, similar to VanRS but more closely related to a family of two-component regulators linked to VanY-like carboxypeptidases in several glycopeptide-susceptible Bacillus species. This upstream region also included a transposase similar to a transposase found in Bacillus halodurans and, in some strains, a 99-bp insertion of unknown function with 95% nucleotide identity to a portion of the Tn1546 transposase gene. Analysis of glycopeptide resistance-associated clusters from soil and/or insect-dwelling organisms may provide important clues to the molecular evolution of acquired glycopeptide resistance elements in human pathogens.

scholarly journals Mechanistic Dissection of the Enzyme Complexes Involved in Biosynthesis of Lacticin 3147 and Nisin

2008 ◽  
Vol 74 (21) ◽  
pp. 6591-6597 ◽  
Author(s):  
Anneke Kuipers ◽  
Jenny Meijer-Wierenga ◽  
Rick Rink ◽  
Leon D. Kluskens ◽  
Gert N. Moll
Keyword(s):  
Lactococcus Lactis ◽  
Bifunctional Enzyme ◽  
Bifunctional Enzymes ◽  
Lacticin 3147 ◽  
Two Component ◽  
Modified Peptides ◽  
Enzyme Complexes ◽  
Insight Into ◽  
Design And Production

ABSTRACT The thioether rings in the lantibiotics lacticin 3147 and nisin are posttranslationally introduced by dehydration of serines and threonines, followed by coupling of these dehydrated residues to cysteines. The prepeptides of the two-component lantibiotic lacticin 3147, LtnA1 and LtnA2, are dehydrated and cyclized by two corresponding bifunctional enzymes, LtnM1 and LtnM2, and are subsequently processed and exported via one bifunctional enzyme, LtnT. In the nisin synthetase complex, the enzymes NisB, NisC, NisT, and NisP dehydrate, cyclize, export, and process prenisin, respectively. Here, we demonstrate that the combination of LtnM2 and LtnT can modify, process, and transport peptides entirely different from LtnA2 and that LtnT can process and transport unmodified LtnA2 and unrelated peptides. Furthermore, we demonstrate a higher extent of NisB-mediated dehydration in the absence of thioether rings. Thioether rings apparently inhibited dehydration, which implies alternating actions of NisB and NisC. Furthermore, certain (but not all) NisC-cyclized peptides were exported with higher efficiency as a result of their conformation. Taken together, these data provide further insight into the applicability of Lactococcus lactis strains containing lantibiotic enzymes for the design and production of modified peptides.

Stress Response Kinetics of Two Nisin Producer Strains of Lactococcus lactis spp. lactis

2008 ◽  
Vol 158 (2) ◽  
pp. 387-397 ◽  
Author(s):  
Ömer Şimşek ◽  
Sencer Buzrul ◽  
Nefise Akkoç ◽  
Hami Alpas ◽  
Mustafa Akçelik
Keyword(s):  
Stress Response ◽  
Lactococcus Lactis ◽  
Kinetics Of ◽  
Nisin Producer ◽  
Producer Strains

scholarly journals Two nucleoside transporters in Lactococcus lactis with different substrate specificities

Microbiology ◽  
2010 ◽  
Vol 156 (10) ◽  
pp. 3148-3157 ◽  
Author(s):  
Jan Martinussen ◽  
Claus Sørensen ◽  
Christian Bille Jendresen ◽  
Mogens Kilstrup
Keyword(s):  
Lactococcus Lactis ◽  
Abc Transporter ◽  
Nucleoside Transporters ◽  
Physiological Level ◽  
Substrate Specificities ◽  
Pyrimidine Nucleosides ◽  
High Affinity ◽  
Phosphorylated Compounds ◽  
Genes Encoding ◽  
Do So

In an alternative to biosynthesis of nucleotides, most organisms are capable of exploiting exogenous nucleotide sources. In order to do so, the nucleotide precursors must pass the membrane, which requires the presence of transporters. Normally, phosphorylated compounds are not subject to transport, and the utilization of nucleotides is dependent on exogenous phosphatases. The composition of transporters with specificity for purine and pyrimidine nucleosides and nucleobases is subject to variation. The ability of Lactococcus lactis to transport different nucleosides across the cell membrane was characterized at both genetic and physiological level, using mutagenesis and by measuring the growth and uptake of nucleosides in the different mutants supplemented with different nucleosides. Two high affinity transporters were identified: BmpA–NupABC was shown to be an ABC transporter with the ability to actively transport all common nucleosides, whereas UriP was shown to be responsible for the uptake of only uridine and deoxyuridine. Interestingly, the four genes encoding the ABC transporter were found at different positions on the chromosome. The bmpA gene was separated from the nupABC operon by 60 kb. Moreover, bmpA was subject to regulation by purine availability, whereas the nupABC operon was constitutively expressed.

scholarly journals Regulation of tartrate metabolism by TtdR and relation to the DcuS–DcuR-regulated C4-dicarboxylate metabolism of Escherichia coli

Microbiology ◽  
2009 ◽  
Vol 155 (11) ◽  
pp. 3632-3640 ◽  
Author(s):  
Ok Bin Kim ◽  
Julia Reimann ◽  
Hanna Lukas ◽  
Uwe Schumacher ◽  
Jan Grimpo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Promoter Region ◽  
Anaerobic Conditions ◽  
Two Component System ◽  
Two Component ◽  
Fumarate Respiration ◽  
Mutual Regulation ◽  
Genes Encoding ◽  
Type Gene ◽  
Tartrate Dehydratase

Escherichia coli catabolizes l-tartrate under anaerobic conditions to oxaloacetate by the use of l-tartrate/succinate antiporter TtdT and l-tartrate dehydratase TtdAB. Subsequently, l-malate is channelled into fumarate respiration and degraded to succinate by the use of fumarase FumB and fumarate reductase FrdABCD. The genes encoding the latter pathway (dcuB, fumB and frdABCD) are transcriptionally activated by the DcuS–DcuR two-component system. Expression of the l-tartrate-specific ttdABT operon encoding TtdAB and TtdT was stimulated by the LysR-type gene regulator TtdR in the presence of l- and meso-tartrate, and repressed by O2 and nitrate. Anaerobic expression required a functional fnr gene, and nitrate repression depended on NarL and NarP. Expression of ttdR, encoding TtdR, was repressed by O2, nitrate and glucose, and positively regulated by TtdR and DcuS. Purified TtdR specifically bound to the ttdR–ttdA promoter region. TtdR was also required for full expression of the DcuS–DcuR-dependent dcuB gene in the presence of tartrate. Overall, expression of the ttdABT genes is subject to l-/meso-tartrate-dependent induction, and to aerobic and nitrate repression. The control is exerted directly at ttdA and in addition indirectly by regulating TtdR levels. TtdR recognizes a subgroup (l- and meso-tartrate) of the stimuli perceived by the sensor DcuS, which responds to all C4-dicarboxylates; both systems apparently communicate by mutual regulation of the regulatory genes.

scholarly journals Pseudomonas syringae Two-Component Response Regulator RhpR Regulates Promoters Carrying an Inverted Repeat Element

2010 ◽  
Vol 23 (7) ◽  
pp. 927-939 ◽  
Author(s):  
Xin Deng ◽  
Lefu Lan ◽  
Yanmei Xiao ◽  
Megan Kennelly ◽  
Jian-Min Zhou ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Inverted Repeat ◽  
Response Regulator ◽  
Effector Proteins ◽  
Dependent Manner ◽  
Type Iii ◽  
Regulatory Cascade ◽  
Two Component ◽  
Genes Encoding ◽  
Element Activity

The two-component system RhpRS was identified in Pseudomonas syringae as a regulator of the genes encoding the type III secretion system and type III effector proteins (together called the T3 genes). In the absence of the sensor kinase RhpS, the response regulator RhpR represses the induction of the T3 gene regulatory cascade consisting of hrpRS, hrpL, and the T3 genes in a phosphorylation-dependent manner. The repressor activity of RhpR is inhibited by RhpS, which presumably acts as a phosphatase under the T3 gene inducing conditions. Here, we show that RhpR binds and induces its own promoter in a phosphorylation-dependent manner. Deletion and mutagenesis analyses revealed an inverted repeat (IR) element, GTATC-N6-GATAC, in the rhpR promoter that confers the RhpR-dependent induction. Computational search of the P. syringae genomes for the putative IR elements and Northern blot analysis of the genes with a putative IR element in the promoter region uncovered five genes that were upregulated and two genes that were downregulated in an RhpR-dependent manner. Two genes that were strongly induced by RhpR were assayed for the IR element activity in gene regulation and, in both cases, the IR element mediated the RhpR-dependent gene induction. Chromatin immunoprecipitation assays indicated that RhpR binds the promoters containing a putative IR element but not the hrpR and hrpL promoters that do not have an IR element, suggesting that RhpR indirectly regulates the transcriptional cascade of hrpRS, hrpL, and the T3 genes.

scholarly journals Inactivation of an Iron Transporter in Lactococcus lactis Results in Resistance to Tellurite and Oxidative Stress

2007 ◽  
Vol 73 (19) ◽  
pp. 6144-6149 ◽  
Author(s):  
Mark S. Turner ◽  
Yu Pei Tan ◽  
Philip M. Giffard
Keyword(s):  
Oxidative Stress ◽  
Lactococcus Lactis ◽  
Oxygen Toxicity ◽  
Phosphate Transport ◽  
Lag Phase ◽  
Uptake System ◽  
Wild Type ◽  
Oxidative Defense ◽  
Genes Encoding ◽  
Resistant Mutants

ABSTRACT In Lactococcus lactis, the interactions between oxidative defense, metal metabolism, and respiratory metabolism are not fully understood. To provide an insight into these processes, we isolated and characterized mutants of L. lactis resistant to the oxidizing agent tellurite (TeO3 2−), which generates superoxide radicals intracellularly. A collection of tellurite-resistant mutants was obtained using random transposon mutagenesis of L. lactis. These contained insertions in genes encoding a proton-coupled Mn2+/Fe2+ transport homolog (mntH), the high-affinity phosphate transport system (pstABCDEF), a putative osmoprotectant uptake system (choQ), and a homolog of the oxidative defense regulator spx (trmA). The tellurite-resistant mutants all had better survival than the wild type following aerated growth. The mntH mutant was found to be impaired in Fe2+ uptake, suggesting that MntH is a Fe2+ transporter in L. lactis. This mutant is capable of carrying out respiration but does not generate as high a final pH and does not exhibit the long lag phase in the presence of hemin and oxygen that is characteristic of wild-type L. lactis. This study suggests that tellurite-resistant mutants also have increased resistance to oxidative stress and that intracellular Fe2+ can heighten tellurite and oxygen toxicity.

Immobilization of nisin producer Lactococcus lactis strains to chitin with surface-displayed chitin-binding domain

2013 ◽  
Vol 97 (10) ◽  
pp. 4577-4587 ◽  
Author(s):  
Ömer Şimşek ◽  
Seba Sabanoğlu ◽  
Ahmet Hilmi Çon ◽  
Nihat Karasu ◽  
Mustafa Akçelik ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Binding Domain ◽  
Chitin Binding Domain ◽  
Nisin Producer
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