Structural Basis for Natural Product Selection and Export by Bacterial ABC Transporters (235 views)
Acs Chemical Biology, 2018 Jun; 13(6): 1598-1609.
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Paper type: Journal Article,
Impact factor: 4.374, 5-year impact factor: 4.991
Url: https://pubmed.ncbi.nlm.nih.gov/29757605/
Keywords: Atp Binding Cassette, Microcin J25, Anti-Bacterial Agents, Lasso Peptides, Nuclear Magnetic Resonance Biomolecular, Protein Transport,
Affiliations:
*** IBB - CNR ***
Department of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
Rutherford Appleton Laboratory, Research Complex at Harwell, Oxfordshire OX11 0DE , United Kingdom.
Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.
Communication Molecules and Adaptation of Microorganisms Laboratory (MCAM, UMR 7245 CNRS-MNHN), Sorbonne Universités, Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique, CP 54, 57 rue Cuvier 75005 Paris, France.
Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign, 600 S. Mathews Avenue, Urbana, Illinois 61801, United States.
Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Université Paris-Sud, Université Paris-Saclay, 1 av. de la Terrasse, 91198 Gif-sur-Yvette, France.
References:
Not available.
Acs Chemical Biology, 2018 Jun; 13(6): 1598-1609.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.374, 5-year impact factor: 4.991
Url: https://pubmed.ncbi.nlm.nih.gov/29757605/
Keywords: Atp Binding Cassette, Microcin J25, Anti-Bacterial Agents, Lasso Peptides, Nuclear Magnetic Resonance Biomolecular, Protein Transport,
Affiliations:
*** IBB - CNR ***
Department of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
Rutherford Appleton Laboratory, Research Complex at Harwell, Oxfordshire OX11 0DE , United Kingdom.
Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.
Communication Molecules and Adaptation of Microorganisms Laboratory (MCAM, UMR 7245 CNRS-MNHN), Sorbonne Universités, Muséum National d'Histoire Naturelle, Centre National de la Recherche Scientifique, CP 54, 57 rue Cuvier 75005 Paris, France.
Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign, 600 S. Mathews Avenue, Urbana, Illinois 61801, United States.
Institut de Chimie des Substances Naturelles, CNRS UPR 2301, Université Paris-Sud, Université Paris-Saclay, 1 av. de la Terrasse, 91198 Gif-sur-Yvette, France.
References:
Not available.
Structural Basis for Natural Product Selection and Export by Bacterial ABC Transporters
Bacteria under stress produce ribosomally synthesized and post-translationally modified peptides (RiPPs) to target closely related species, such as the lasso peptide microcin J25 (MccJ25). These peptides are also toxic to the producing organisms that utilize dedicated ABC transporters to achieve self-immunity. MccJ25 is exported by the Escherichia coli ABC transporter McjD through a complex mechanism of recognition that has remained elusive. Here, we used biomolecular NMR to study this interaction and identified a region of the toxic peptide that is crucial to its recognition by the ABC transporter. Our study provides evidence that McjD is highly specific to MccJ25 and not to other RiPPs or antibiotics, unlike multidrug ABC transporters. Additionally, we show that MccJ25 is not exported by another natural product ABC transporter. Therefore, we propose that specific interactions between natural product ABC transporters and their substrate provides them with their high degree of specificity. Taken together, these findings suggest that ABC transporters might have acquired structural elements in their binding cavity to recognize and allow promiscuous export of a larger variety of compounds.
Bacteria under stress produce ribosomally synthesized and post-translationally modified peptides (RiPPs) to target closely related species, such as the lasso peptide microcin J25 (MccJ25). These peptides are also toxic to the producing organisms that utilize dedicated ABC transporters to achieve self-immunity. MccJ25 is exported by the Escherichia coli ABC transporter McjD through a complex mechanism of recognition that has remained elusive. Here, we used biomolecular NMR to study this interaction and identified a region of the toxic peptide that is crucial to its recognition by the ABC transporter. Our study provides evidence that McjD is highly specific to MccJ25 and not to other RiPPs or antibiotics, unlike multidrug ABC transporters. Additionally, we show that MccJ25 is not exported by another natural product ABC transporter. Therefore, we propose that specific interactions between natural product ABC transporters and their substrate provides them with their high degree of specificity. Taken together, these findings suggest that ABC transporters might have acquired structural elements in their binding cavity to recognize and allow promiscuous export of a larger variety of compounds.
Structural Basis for Natural Product Selection and Export by Bacterial ABC Transporters
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Structural Basis for Natural Product Selection and Export by Bacterial ABC Transporters
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Berisio R, Corti N, Pfister P, Yonath A, Böttger EC
* 23S rRNA 2058A→G alteration mediates ketolide resistance in combination with deletion in L22 (751 views)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2006 Nov; 50(11): 3816-3823.
Impact Factor: 4.153
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Agmon I, Amit M, Auerbach T, Bashan A, Baram D, Bartels H, Berisio R, Greenberg I, Harms J, Hansen HAS, Kessler M, Pyetan E, Schluenzen F, Sittner A, Yonath A, Zarivach R
* Ribosomal crystallography: A flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism (387 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2004 Jun 1; 567(1): 20-26.
Impact Factor: 3.843
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Saviano M, Improta R, Benedetti E, Carrozzini B, Cascarano GL, Didierjean C, Toniolo C, Crisma M
* Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue (487 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Apr 2; 5(4): 541-544.
Impact Factor: 3.474
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Bashan A, Zarivach R, Schluenzen F, Agmon I, Harms J, Auerbach T, Baram D, Berisio R, Bartels H, Hansen HAS, Fucini P, Wilson D, Peretz M, Kessler M, Yonath A
* Ribosomal crystallography: Peptide bond formation and its inhibition (641 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003 Sep; 70(1): 19-41.
Impact Factor: 2.733
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Berisio R, Harms J, Schluenzen F, Zarivach R, Hansen HAS, Fucini P, Yonath A
* Structural insight into the antibiotic action of telithromycin against resistant mutants (510 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Impact Factor: 4.175
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Monti SM, Fogliano V, Logrieco A, Ferracane R, Ritieni A
Simultaneous determination of beauvericin, enniatins, and fusaproliferin by high performance liquid chromatography (573 views)
J Agric Food Chem (ISSN: 0021-8561), 2000 Sep; 48(8): 3317-3320.
Impact Factor: 1.56
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26 Records (25 excluding Abstracts).
Total impact factor: 166.207 (161.856 excluding Abstracts).
Total 5 year impact factor: 166.366 (161.983 excluding Abstracts).
Total impact factor: 166.207 (161.856 excluding Abstracts).
Total 5 year impact factor: 166.366 (161.983 excluding Abstracts).
235 views. Last view on Friday 13 September 2024, 13:28:01
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