Functional and structural characterization of a prokaryotic peptide transporter with features similar to mammalian PEPT1

Weitz, Dietmar; Harder, Daniel; Casagrande, Fabio; Fotiadis, Dimitrios; Obrdlik, Petr; Kelety, Bela; Daniel, Hannelore (2007). Functional and structural characterization of a prokaryotic peptide transporter with features similar to mammalian PEPT1. Journal of biological chemistry, 282(5), pp. 2832-9. Bethesda, Md.: American Society for Biochemistry and Molecular Biology 10.1074/jbc.M604866200

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The ydgR gene of Escherichia coli encodes a protein of the proton-dependent oligopeptide transporter (POT) family. We cloned YdgR and overexpressed the His-tagged fusion protein in E. coli BL21 cells. Bacterial growth inhibition in the presence of the toxic phosphonopeptide alafosfalin established YgdR functionality. Transport was abolished in the presence of the proton ionophore carbonyl cyanide p-chlorophenylhydrazone, suggesting a proton-coupled transport mechanism. YdgR transports selectively only di- and tripeptides and structurally related peptidomimetics (such as aminocephalosporins) with a substrate recognition pattern almost identical to the mammalian peptide transporter PEPT1. The YdgR protein was purified to homogeneity from E. coli membranes. Blue native-polyacrylamide gel electrophoresis and transmission electron microscopy of detergent-solubilized YdgR suggest that it exists in monomeric form. Transmission electron microscopy revealed a crown-like structure with a diameter of approximately 8 nm and a central density. These are the first structural data obtained from a proton-dependent peptide transporter, and the YgdR protein seems an excellent model for studies on substrate and inhibitor interactions as well as on the molecular architecture of cell membrane peptide transporters.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Fotiadis, Dimitrios José

ISSN:

0021-9258

ISBN:

17158458

Publisher:

American Society for Biochemistry and Molecular Biology

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:53

Last Modified:

04 May 2014 23:15

Publisher DOI:

10.1074/jbc.M604866200

PubMed ID:

17158458

Web of Science ID:

000243793900009

URI:

https://boris.unibe.ch/id/eprint/22703 (FactScience: 36081)

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