Di-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis.

TitleDi-tripeptides and oligopeptides are taken up via distinct transport mechanisms in Lactococcus lactis.
Publication TypeJournal Article
Year of Publication1993
AuthorsKunji, ERS, Smid, EJ, Plapp, R, Poolman, B, Konings, WN
JournalJ Bacteriol
Date Published1993 Apr
KeywordsAdenosine Triphosphate, Amino Acid Sequence, Arsenates, beta-Alanine, Biological Transport, Active, Dipeptides, Drug Resistance, Microbial, Energy Metabolism, Glucose, Lactococcus lactis, Molecular Sequence Data, Molecular Weight, Mutagenesis, Oligopeptides, Substrate Specificity, Vanadates

Lactococcus lactis ML3 possesses two different peptide transport systems of which the substrate size restriction and specificity have been determined. The first system is the earlier-described proton motive force-dependent di-tripeptide carrier (E. J. Smid, A. J. M. Driessen, and W. N. Konings, J. Bacteriol. 171:292-298, 1989). The second system is a metabolic energy-dependent oligopeptide transport system which transports peptides of four to at least six amino acid residues. The involvement of a specific oligopeptide transport system in the utilization of tetra-alanine and penta-alanine was established in a mutant of L. lactis MG1363 that was selected on the basis of resistance to toxic analogs of alanine and alanine-containing di- and tripeptides. This mutant is unable to transport alanine, dialanine, and trialanine but still shows uptake of tetra-alanine and penta-alanine. The oligopeptide transport system has a lower activity than the di-tripeptide transport system. Uptake of oligopeptides occurs in the absence of a proton motive force and is specifically inhibited by vanadate. The oligopeptide transport system is most likely driven by ATP or a related energy-rich, phosphorylated intermediate.

Alternate JournalJ. Bacteriol.
Citation Key10.1128/jb.175.7.2052-2059.1993
PubMed ID8458848
PubMed Central IDPMC204299