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The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane
J. Felix, L. Bumba, C. Liesche, A. Fraudeau, F. Rébeillé, JY. El Khoury, K. Huard, B. Gallet, C. Moriscot, JP. Kleman, Y. Duhoo, M. Jessop, E. Kandiah, F. Barras, J. Jouhet, I. Gutsche
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články
Grantová podpora
ALTF441-2017
European Molecular Biology Organization (EMBO)
RespViRALI
EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 Marie Skłodowska-Curie Actions (H2020 Excellent Science - Marie Skłodowska-Curie Actions)
647784
EC | EU Framework Programme for Research and Innovation H2020 | H2020 Excellent Science (H2020 Priority Excellent Science)
ANR-10-INSB-05-01
Agence Nationale de la Recherche (French National Research Agency)
ANR-10-INBS-0005-02
French Infrastructure for Integrated Structural Biology (FRISBI)
NLK
Directory of Open Access Journals
od 2015
Free Medical Journals
od 2010
Nature Open Access
od 2010-12-01
PubMed Central
od 2012
Europe PubMed Central
od 2012
ProQuest Central
od 2010-01-01
Open Access Digital Library
od 2015-01-01
Open Access Digital Library
od 2015-01-01
Medline Complete (EBSCOhost)
od 2012-11-01
Health & Medicine (ProQuest)
od 2010-01-01
ROAD: Directory of Open Access Scholarly Resources
od 2010
Springer Nature OA/Free Journals
od 2010-12-01
- MeSH
- adenosintrifosfatasy * metabolismus MeSH
- aminoglykosidy * farmakologie MeSH
- antibakteriální látky farmakologie MeSH
- ATPázy spojené s různými buněčnými aktivitami metabolismus MeSH
- Escherichia coli * účinky léků enzymologie MeSH
- fosfolipidy MeSH
- fumaráty MeSH
- gentamiciny MeSH
- kyslík metabolismus MeSH
- membránové lipidy MeSH
- proteiny z Escherichia coli * metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
Enteric bacteria have to adapt to environmental stresses in the human gastrointestinal tract such as acid and nutrient stress, oxygen limitation and exposure to antibiotics. Membrane lipid composition has recently emerged as a key factor for stress adaptation. The E. coli ravA-viaA operon is essential for aminoglycoside bactericidal activity under anaerobiosis but its mechanism of action is unclear. Here we characterise the VWA domain-protein ViaA and its interaction with the AAA+ ATPase RavA, and find that both proteins localise at the inner cell membrane. We demonstrate that RavA and ViaA target specific phospholipids and subsequently identify their lipid-binding sites. We further show that mutations abolishing interaction with lipids restore induced changes in cell membrane morphology and lipid composition. Finally we reveal that these mutations render E. coli gentamicin-resistant under fumarate respiration conditions. Our work thus uncovers a ravA-viaA-based pathway which is mobilised in response to aminoglycosides under anaerobiosis and engaged in cell membrane regulation.
Division of Structural Biology The Institute of Cancer Research London UK
EMBL Grenoble 71 Avenue des martyrs Grenoble France
European Synchrotron Radiation Facility 71 Avenue des martyrs Grenoble France
Unit for Structural Biology VIB UGent Center for Inflammation Research Ghent Belgium
Univ Grenoble Alpes CEA CNRS ISBG 71 Avenue des martyrs Grenoble France
Citace poskytuje Crossref.org
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- $a Enteric bacteria have to adapt to environmental stresses in the human gastrointestinal tract such as acid and nutrient stress, oxygen limitation and exposure to antibiotics. Membrane lipid composition has recently emerged as a key factor for stress adaptation. The E. coli ravA-viaA operon is essential for aminoglycoside bactericidal activity under anaerobiosis but its mechanism of action is unclear. Here we characterise the VWA domain-protein ViaA and its interaction with the AAA+ ATPase RavA, and find that both proteins localise at the inner cell membrane. We demonstrate that RavA and ViaA target specific phospholipids and subsequently identify their lipid-binding sites. We further show that mutations abolishing interaction with lipids restore induced changes in cell membrane morphology and lipid composition. Finally we reveal that these mutations render E. coli gentamicin-resistant under fumarate respiration conditions. Our work thus uncovers a ravA-viaA-based pathway which is mobilised in response to aminoglycosides under anaerobiosis and engaged in cell membrane regulation.
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