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Two ABC transport systems carry out peptide uptake in Enterococcus faecalis: Their roles in growth and in uptake of sex pheromones
Department of Microbiology and Immunology, University of Minnesota Medical School, MN, Minneapolis, United States.
Department of Microbiology and Immunology, University of Minnesota Medical School, MN, Minneapolis, United States; Recursion, UT, Salt Lake City, United States.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics. Umeå University, Faculty of Medicine, Wallenberg Centre for Molecular Medicine at Umeå University (WCMM).ORCID iD: 0000-0001-6848-322x
Department of Microbiology and Immunology, University of Minnesota Medical School, MN, Minneapolis, United States.
2021 (English)In: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 116, no 2, p. 459-469Article in journal (Refereed) Published
Abstract [en]

Enterococcal pheromone-inducible plasmids encode a predicted OppA-family secreted lipoprotein. In the case of plasmid pCF10, the protein is PrgZ, which enhances the mating response to cCF10 pheromone. OppA proteins generally function with associated OppBCDF ABC transporters to import peptides. In this study, we analyzed the potential interactions of PrgZ with two host-encoded Opp transporters using two pheromone-inducible fluorescent reporter constructs. Based on our results, we propose renaming these loci opp1 (OG1RF_10634-10639) and opp2 (OG1RF_12366-12370). We also examined the ability of the Opp1 and Opp2 systems to mediate import in the absence of PrgZ. Cells expressing PrgZ were able to import pheromone if either opp1 or opp2 was functional, but not if both opp loci were disrupted. In the absence of PrgZ, pheromone import was dependent on a functional opp2 system, including opp2A. Comparative structural analysis of the peptide-binding pockets of PrgZ, Opp1A, Opp2A, and the related Lactococcus lactis OppA protein, suggested that the robust pheromone-binding ability of PrgZ relates to a nearly optimal fit of the hydrophobic peptide, whereas binding ability of Opp2A likely results from a more open, promiscuous peptide-binding pocket similar to L. lactis OppA.

Place, publisher, year, edition, pages
John Wiley & Sons, 2021. Vol. 116, no 2, p. 459-469
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-183010DOI: 10.1111/mmi.14725ISI: 000641087500001PubMedID: 33817866Scopus ID: 2-s2.0-85104404314OAI: oai:DiVA.org:umu-183010DiVA, id: diva2:1554732
Funder
Swedish Research Council, 2016-03599Knut and Alice Wallenberg FoundationAvailable from: 2021-05-17 Created: 2021-05-17 Last updated: 2022-02-24Bibliographically approved

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Berntsson, Ronnie Per-Arne

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Department of Medical Biochemistry and BiophysicsWallenberg Centre for Molecular Medicine at Umeå University (WCMM)
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