Literature DB >> 12590143

Diversity of oligopeptide transport specificity in Lactococcus lactis species. A tool to unravel the role of OppA in uptake specificity.

Pascale Charbonnel1, Mauld Lamarque, Jean-Christophe Piard, Christophe Gilbert, Vincent Juillard, Danièle Atlan.   

Abstract

The specific oligopeptide transport system Opp is essential for growth of Lactococcus lactis in milk. We examined the biodiversity of oligopeptide transport specificity in the L. lactis species. Six strains were tested for (i) consumption of peptides during growth in a chemically defined medium and (ii) their ability to transport these peptides. Each strain demonstrated some specific preferences for peptide utilization, which matched the specificity of peptide transport. Sequencing of the binding protein OppA in some strains revealed minor differences at the amino acid level. The differences in specificity were used as a tool to unravel the role of the binding protein in transport specificity. The genes encoding OppA in four strains were cloned and expressed in L. lactis MG1363 deleted for its oppA gene. The substrate specificity of these engineered strains was found to be similar to that of the L. lactis MG1363 parental strain, whichever oppA gene was expressed. In situ binding experiments demonstrated the ability of OppA to interact with non-transported peptides. Taken together, these results provide evidence for a new concept. Despite that fact that OppA is essential for peptide transport, it is not the (main) determinant of peptide transport specificity in L. lactis.

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Year:  2003        PMID: 12590143     DOI: 10.1074/jbc.M212454200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  9 in total

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Authors:  Xing-Guo Wang; J Michael Kidder; Joanna P Scagliotti; Mark S Klempner; Richard Noring; Linden T Hu
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Review 5.  Structure, function, and evolution of bacterial ATP-binding cassette systems.

Authors:  Amy L Davidson; Elie Dassa; Cedric Orelle; Jue Chen
Journal:  Microbiol Mol Biol Rev       Date:  2008-06       Impact factor: 11.056

6.  A multifunction ABC transporter (Opt) contributes to diversity of peptide uptake specificity within the genus Lactococcus.

Authors:  Mauld Lamarque; Pascale Charbonnel; Dominique Aubel; Jean-Christophe Piard; Danièle Atlan; Vincent Juillard
Journal:  J Bacteriol       Date:  2004-10       Impact factor: 3.490

7.  Identification of a differentially expressed oligopeptide binding protein (OppA2) in Streptococcus uberis by representational difference analysis of cDNA.

Authors:  D L Taylor; P N Ward; C D Rapier; J A Leigh; L D Bowler
Journal:  J Bacteriol       Date:  2003-09       Impact factor: 3.490

8.  pH- and Temperature-Dependent Peptide Binding to the Lactococcus lactis Oligopeptide-Binding Protein A Measured with a Fluorescence Anisotropy Assay.

Authors:  Stevie Norcross; Ashwin Sunderraj; Mathew Tantama
Journal:  ACS Omega       Date:  2019-02-06

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  9 in total

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