Article Abstract:
The gene encoding the di- and tripeptide transport protein (DtpT) of Lactobacillus helveticus (DtpT(sub SH)) was cloned with the help of the inverse PCR method and employed to complement the dipeptide transport-deficient and proline-auxotrophic Escherichia coli E1772. The dtpT(sub SH) gene is composed of 1,491 bp, which translates into a 497-amino-acid polypeptide. DtpT(sub SH) has 34% similarity to the di- and tripeptide transport protein of Lactococcus lactis and is also homologous to various peptide transporters of eukaryotic origin.
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Article Abstract:
Protein transport in Saccharomyces cerevisiae operate primarily through the extensive fluxing of lipids from intracellular organelles to the plasma membrane. The transport is facilitated by the hydrolysis of ATP molecules by the plasma membrane to generate a proton motive force that will fuel secondary transport processes. In S. cerevisiae, transport activity may proceed via uniport systems or via proton symport systems. Both are regulated at the transcription level.
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Article Abstract:
The inverse PCR method was utilized in an experiment to clone the gene that encodes the di- and tripeptide transport protein of Lactobacillus helveticus. In addition, the functional expression in an Escherichia coli protein was evaluated. Results show that the proton motive force affects peptide transport through DtpT in membrane vesicles. The specificity for di-and tripeptides is not applicable to tetrapeptides or amino acids.
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