Cloning and functional expression in Escherichia coli of the gene encoding the di- and tripeptide transport protein of Lactobacillus helveticus.

TitleCloning and functional expression in Escherichia coli of the gene encoding the di- and tripeptide transport protein of Lactobacillus helveticus.
Publication TypeJournal Article
Year of Publication1997
AuthorsNakajima, H, Hagting, A, Kunji, ERS, Poolman, B, Konings, WN
JournalAppl Environ Microbiol
Volume63
Issue6
Pagination2213-7
Date Published1997 Jun
ISSN0099-2240
KeywordsAmino Acid Sequence, Bacterial Proteins, Base Sequence, Biological Transport, Active, Carrier Proteins, Cloning, Molecular, Dipeptides, DNA, Bacterial, Escherichia coli, Gene Expression, Genes, Bacterial, Kinetics, Lactobacillus, Membrane Transport Proteins, Molecular Sequence Data, Oligopeptides, Sequence Homology, Amino Acid
Abstract

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.

Alternate JournalAppl. Environ. Microbiol.
Citation Key1138
PubMed ID9172341
PubMed Central IDPMC168514