Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis

Tynkkynen, Soile; Buist, Girbe; Kunji, Edmund R. S.; Kok, Jan; Poolman, Berend; Venema, Gerard; Haandrikman, Alfred J.

doi:10.1128/jb.175.23.7523-7532.1993

Cited by 201 publications

(197 citation statements)

References 58 publications

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“…Comparable findings were made with neutral glycine-containing peptides, i.e., X-Gly and Gly-X. Since the oligopeptide transport system is specific for peptides containing at least four residues (29), the defect in the uptake of charged and Gly-containing neutral dipeptides in the double mutant must be the result of the dtpT mutation. On the other hand, Phe-containing peptides were transported by L. lactis CV4, albeit at reduced rates compared with that for the wild-type MG1363.…”

Section: Utilization Of Peptides By L Lactis Strains During Growthmentioning

confidence: 95%

“…The oligopeptide permeases (Opp) of Escherichia coli and Salmonella typhimurium handle any peptide containing two to six amino acids, whereas the Opp system of L. lactis transports peptides of four to at least eight amino acid residues (29). The dipeptide permeases (Dpp) of E. coli and S. typhimurium are relatively specific for dipeptides, whereas the tripeptide permeases (Tpp) possess the highest affinity for hydrophobic tripeptides.…”

Section: Discussionmentioning

confidence: 99%

“…The peptide transport systems of enteric bacteria belong to the family of binding-protein-dependent transport systems that are composed of multiple subunits and use (most likely) ATP to drive transport (7). The Opp system of L. lactis also belongs to this family of transporters (29). On the contrary, the di-and tripeptide carrier (DtpT) of L. lactis is a secondary transport system which uses the proton motive force to accumulate peptides (6,25).…”

Section: Discussionmentioning

confidence: 99%

“…L. lactis subsp. lactis MG1363 wild-type and isogenic mutants, i.e., the di-and tripeptide transport mutant AG300, the oligopeptide transport mutant VS772, and the peptide transport double mutant CV4, have been described previously (6,11,29) and are presented in Table 1. Strains were grown at 30ЊC in M17 broth (27) or in a CDM (19) at pH 6.8 supplemented with 0.5% (wt/vol) glucose or 0.5% (wt/vol) maltose in combination with 25 mM arginine to induce the arginine deiminase pathway (17).…”

Section: Methodsmentioning

confidence: 99%

“…At present, two peptide transport systems have been characterized for Lactococcus lactis (6,10,11,29). The oligopeptide transport system (Opp) mediates the ATP-driven transport of peptides with four to at least eight residues.…”

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Specificity of peptide transport systems in Lactococcus lactis: evidence for a third system which transports hydrophobic di- and tripeptides

et al. 1995

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A proton motive force-driven di-tripeptide carrier protein (DtpT) and an ATP-dependent oligopeptide transport system (Opp) have been described for Lactococcus lactis MG1363. Using genetically well-defined mutants in which dtpT and/or opp were inactivated, we have now established the presence of a third peptide transport system (DtpP) in L. lactis. The specificity of DtpP partially overlaps that of DtpT. DtpP transports preferentially di-and tripeptides that are composed of hydrophobic (branched-chain amino acid) residues, whereas DtpT has a higher specificity for more-hydrophilic and charged peptides. The toxic dipeptide L-phenylalanyl-␤-chloro-L-alanine has been used to select for a di-tripeptide transport-negative mutant with the ⌬dtpT strain as a genetic background. This mutant is unable to transport di-and tripeptides but still shows uptake of amino acids and oligopeptides. The DtpP system is induced in the presence of di-and tripeptides containing branched-chain amino acids. The use of ionophores and metabolic inhibitors suggests that, similar to Opp, DtpP-mediated peptide transport is driven by ATP or a related energy-rich phosphorylated intermediate.For optimal growth in milk, lactococci depend on the presence of a proteolytic system which consists of a cell envelopelocated proteinase, several peptidases, and amino acid and peptide transport systems (20). At present, two peptide transport systems have been characterized for Lactococcus lactis (6,10,11,29). The oligopeptide transport system (Opp) mediates the ATP-driven transport of peptides with four to at least eight residues. It plays a central role in the proteolytic pathway of L. lactis, as it is essential for the accumulation of all ␤-caseinderived amino acids (10). The level of activity in the Opp system is sufficiently high to support maximal growth rates on ␤-casein, provided that leucine and histidine are present in the medium as free amino acids. The di-and tripeptide transport system (DtpT) is unique among bacterial peptide transporters, as it is encoded by a single gene and uses the proton motive force to drive the transport of relatively hydrophilic di-and tripeptides (6). Spontaneous mutations which inactivate the dtpT gene lead to defective growth of L. lactis in chemically defined medium (CDM) supplemented with a mixture of caseins as the sole source of nitrogen (24).On the basis of the observation that the transport of some di-and tripeptides is totally abolished in alanyl-␤-chloroalanine-resistant mutants of L. lactis whereas other peptides are still taken up at significant rates (26), the utilization of di-and tripeptides in mutants lacking either Opp or DtpT or both peptide transport systems was investigated. In this report, we present evidence for a third peptide transport system in L. lactis with specificity for relatively hydrophobic di-and tripeptides. MATERIALS AND METHODSBacterial strains, culture conditions, and growth media. L. lactis subsp. lactis MG1363 wild-type and isogenic mutants, i.e., the di-and tripeptide transport mut...

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Section: Utilization Of Peptides By L Lactis Strains During Growthmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Specificity of peptide transport systems in Lactococcus lactis: evidence for a third system which transports hydrophobic di- and tripeptides

et al. 1995

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Updates in the Metabolism of Lactic Acid Bacteria

Mayo

Aleksandrzak‐Piekarczyk

Fernández

et al. 2010

Biotechnology of Lactic Acid Bacteria

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Lactic acid bacteria (LAB) are fermentative bacteria naturally dwelling in or intentionally added to nutrient -rich environments where carbohydrates and proteins are usually abundant. The effi cient use of nutrients and the concomitant production of lactic acid during growth endow LAB with remarkable selective advantages in the diverse ecological niches they inhabit. Besides lactic acid, LAB metabolism produces a variety of compounds, such as diacetyl, acetoin and 2 -3 -butanediol from the utilization of citrate, and a vast array of volatile compounds and bioactive peptides from the catabolism of amino acids. The enzymatic reactions of LAB metabolism further modify the organoleptic, rheological, and nutritive properties of the raw materials, giving rise to fi nal fermented products. Last decade witnessed an impressive amount of data on several aspects of LAB physiology and genetics. The latest knowledge was gathered through sequencing and analysis of LAB genomes, and the subsequent use of post -genomic techniques, such as proteomics, comparative genome hybridization, transcriptomics, and metabolomics. Manipulation of the metabolic pathways of LAB to improve their effi ciency in various industrial applications (as starters, adjunct cultures, and probiotics) was undertaken soon after the development of early engineering tools. The availability of complete genome sequences of different LAB species and strains has expanded our ability to further study LAB metabolism from a global perspective, strengthening a full exploitation of LAB ' s metabolic potential.

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Biological traits of lactic acid bacteria: industrial relevance and new perspectives in dairy applications

Mora

Bello²,

Arioli

2017

Microbiology in Dairy Processing

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Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis

Cited by 201 publications

References 58 publications

Specificity of peptide transport systems in Lactococcus lactis: evidence for a third system which transports hydrophobic di- and tripeptides

Specificity of peptide transport systems in Lactococcus lactis: evidence for a third system which transports hydrophobic di- and tripeptides

Updates in the Metabolism of Lactic Acid Bacteria

Biological traits of lactic acid bacteria: industrial relevance and new perspectives in dairy applications

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