Random mutagenesis of the prokaryotic peptide transporter YdgR identifies potential periplasmic gating residues

Malle, Elisabeth, Zhou, Hongwen, Neuhold, Jana, Spitzenberger, Bettina, Klepsch, Freya, Pollak, Thomas, Bergner, Oliver, Ecker, Gerhard F. and Stolt-Bergner, Peggy C. (2011) Random mutagenesis of the prokaryotic peptide transporter YdgR identifies potential periplasmic gating residues. Journal of Biological Chemistry, 286 26: 23121-23131. doi:10.1074/jbc.M111.239657

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Author Malle, Elisabeth
Zhou, Hongwen
Neuhold, Jana
Spitzenberger, Bettina
Klepsch, Freya
Pollak, Thomas
Bergner, Oliver
Ecker, Gerhard F.
Stolt-Bergner, Peggy C.
Title Random mutagenesis of the prokaryotic peptide transporter YdgR identifies potential periplasmic gating residues
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
2152-2561
Publication date 2011-07-01
Sub-type Article (original research)
DOI 10.1074/jbc.M111.239657
Open Access Status File (Publisher version)
Volume 286
Issue 26
Start page 23121
End page 23131
Total pages 11
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Abstract The peptide transporter (PTR) family represents a group of proton-coupled secondary transporters responsible for bulk uptake of amino acids in the form of di- and tripeptides, an essential process employed across species ranging from bacteria to humans. To identify amino acids critical for peptide transport in a prokaryotic PTR member, we have screened a library of mutants of the Escherichia coli peptide transporter YdgR using a high-throughput substrate uptake assay.Wehave identified 35 single point mutations that result in a full or partial loss of transport activity. Additional analysis, including homology modeling based on the crystal structure of the Shewanella oneidensis peptide transporter PepT so, identifies Glu 56 and Arg 305 as potential periplasmic gating residues. In addition to providing new insights into transport by members of the PTR family, these mutants provide valuable tools for further study of the mechanism of peptide transport.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Queensland Brain Institute Publications
 
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