Hagting, Anja

Konings, Wil N.

Kunji, Edmund R.S.

Nakajima, Hajime

Poolman, Bert

English

The gene encoding the di- and tripeptide transport protein (DtpT) of Lactobacillus helveticus (DtpTLH) was cloned with the aid of the inverse PCR technique and used to complement the dipeptide transport-deficient and proline-auxotrophic Escherichia coli E1772. Functional expression of the peptide transporter was shown by the uptake of prolyl-[14C]alanine in whole cells and membrane vesicles. Peptide transport via DtpT in membrane vesicles is driven by the proton motive force. The system has specificity for di- and tripeptides but not for amino acids or tetrapeptides. The dtpTLH gene consists of 1,491 bp, which translates into a 497-amino-acid polypeptide. DtpTLH shows 34% identity to the di- and tripeptide transport protein of Lactococcus lactis and is also homologous to various peptide transporters of eukaryotic origin, but the similarity between these proteins is confined mainly to the N-terminal halves

Dissertations of the University of Groningen

Cloning and Functional Expression in Escherichia coli of the Gene Encoding the Di- and Tripeptide Transport Protein of Lactobacillus helveticus

https://pure.rug.nl/ws/files/3230921/1997ApplEnvironMicrobiolNakajima.pdf

Cloning and Functional Expression in Escherichia coli of the Gene Encoding the Di- and Tripeptide Transport Protein of Lactobacillus helveticus

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Dissertations of the University of Groningen