An RND transporter in the monoterpene metabolism of Castellaniella defragrans.
Identifieur interne : 000635 ( Main/Exploration ); précédent : 000634; suivant : 000636An RND transporter in the monoterpene metabolism of Castellaniella defragrans.
Auteurs : Edinson Puentes-Cala [Allemagne] ; Jens Harder [Allemagne]Source :
- Biodegradation [ 1572-9729 ] ; 2019.
Descripteurs français
- KwdFr :
- Dépollution biologique de l'environnement (MeSH), Famille multigénique (MeSH), Fonctions de vraisemblance (MeSH), Monoterpènes (métabolisme), Monoterpènes (pharmacologie), Phylogenèse (MeSH), Proteobacteria (croissance et développement), Proteobacteria (génétique), Proteobacteria (métabolisme), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Protéines de transport membranaire (métabolisme), Simulation numérique (MeSH).
- MESH :
- croissance et développement : Proteobacteria.
- génétique : Proteobacteria, Protéines bactériennes.
- métabolisme : Monoterpènes, Proteobacteria, Protéines bactériennes, Protéines de transport membranaire.
- pharmacologie : Monoterpènes.
- Dépollution biologique de l'environnement, Famille multigénique, Fonctions de vraisemblance, Phylogenèse, Simulation numérique.
English descriptors
- KwdEn :
- Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Biodegradation, Environmental (MeSH), Computer Simulation (MeSH), Likelihood Functions (MeSH), Membrane Transport Proteins (metabolism), Monoterpenes (metabolism), Monoterpenes (pharmacology), Multigene Family (MeSH), Phylogeny (MeSH), Proteobacteria (genetics), Proteobacteria (growth & development), Proteobacteria (metabolism).
- MESH :
- chemical , genetics : Bacterial Proteins.
- chemical , metabolism : Bacterial Proteins, Membrane Transport Proteins, Monoterpenes.
- chemical , pharmacology : Monoterpenes.
- genetics : Proteobacteria.
- growth & development : Proteobacteria.
- metabolism : Proteobacteria.
- Biodegradation, Environmental, Computer Simulation, Likelihood Functions, Multigene Family, Phylogeny.
Abstract
The betaproteobacterium Castellaniella defragrans 65Phen grows on monoterpenes at concentrations toxic to many bacteria. Tolerance mechanisms include modifications of the membrane fatty acid composition and the mineralization of monoterpenes. In this study, we characterized an efflux transporter associated to the monoterpene metabolism. The inner-membrane transporter AmeD (apolar monoterpene efflux) affiliated to the HAE3 (hydrophobe/amphiphile efflux) family within the Resistance-Nodulation-Division (RND) superfamily. RND pumps of the HAE3 family are known for transporting substrates into the periplasm. AmeD is co-expressed with the outer membrane protein AmeA and the periplasmic proteins AmeB and AmeC, suggesting an export channel into the environment similar to HAE1-type RND exporters. Proteins AmeABCD are encoded within a genetic island involved in the metabolism of acyclic and cyclic monoterpenes. The deletion of ameABCD translated into a decrease in tolerance to monoterpenes in liquid cultures. The addition of acetate as cosubstrate in limonene-containing cultures partially alleviated monoterpene toxicity in the deletion mutant. Accumulation of Nile Red in cells of C. defragrans required dissipation of the proton motive force with carbonyl cyanide m-chlorophenylhydrazone (CCCP). Cells lacking AmeABCD accumulated more Nile Red, suggesting an export function of the proteins. Our observations suggest that the tetrapartite RND transporter AmeABCD acts as an exporter during monoterpene detoxification in C. defragrans.
DOI: 10.1007/s10532-018-9857-6
PubMed: 30334144
PubMed Central: PMC6394551
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xml:lang="fr"><term>Monoterpènes</term><term>Proteobacteria</term><term>Protéines bactériennes</term><term>Protéines de transport membranaire</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Monoterpènes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Computer Simulation</term><term>Likelihood Functions</term><term>Multigene Family</term><term>Phylogeny</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dépollution biologique de l'environnement</term><term>Famille multigénique</term><term>Fonctions de vraisemblance</term><term>Phylogenèse</term><term>Simulation numérique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The betaproteobacterium Castellaniella defragrans 65Phen grows on monoterpenes at concentrations toxic to many bacteria. Tolerance mechanisms include modifications of the membrane fatty acid composition and the mineralization of monoterpenes. In this study, we characterized an efflux transporter associated to the monoterpene metabolism. The inner-membrane transporter AmeD (apolar monoterpene efflux) affiliated to the HAE3 (hydrophobe/amphiphile efflux) family within the Resistance-Nodulation-Division (RND) superfamily. RND pumps of the HAE3 family are known for transporting substrates into the periplasm. AmeD is co-expressed with the outer membrane protein AmeA and the periplasmic proteins AmeB and AmeC, suggesting an export channel into the environment similar to HAE1-type RND exporters. Proteins AmeABCD are encoded within a genetic island involved in the metabolism of acyclic and cyclic monoterpenes. The deletion of ameABCD translated into a decrease in tolerance to monoterpenes in liquid cultures. The addition of acetate as cosubstrate in limonene-containing cultures partially alleviated monoterpene toxicity in the deletion mutant. Accumulation of Nile Red in cells of C. defragrans required dissipation of the proton motive force with carbonyl cyanide m-chlorophenylhydrazone (CCCP). Cells lacking AmeABCD accumulated more Nile Red, suggesting an export function of the proteins. Our observations suggest that the tetrapartite RND transporter AmeABCD acts as an exporter during monoterpene detoxification in C. defragrans.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">30334144</PMID><DateCompleted><Year>2019</Year><Month>04</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1572-9729</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>02</Month></PubDate></JournalIssue><Title>Biodegradation</Title><ISOAbbreviation>Biodegradation</ISOAbbreviation></Journal><ArticleTitle>An RND transporter in the monoterpene metabolism of Castellaniella defragrans.</ArticleTitle><Pagination><MedlinePgn>1-12</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s10532-018-9857-6</ELocationID><Abstract><AbstractText>The betaproteobacterium Castellaniella defragrans 65Phen grows on monoterpenes at concentrations toxic to many bacteria. Tolerance mechanisms include modifications of the membrane fatty acid composition and the mineralization of monoterpenes. In this study, we characterized an efflux transporter associated to the monoterpene metabolism. The inner-membrane transporter AmeD (apolar monoterpene efflux) affiliated to the HAE3 (hydrophobe/amphiphile efflux) family within the Resistance-Nodulation-Division (RND) superfamily. RND pumps of the HAE3 family are known for transporting substrates into the periplasm. AmeD is co-expressed with the outer membrane protein AmeA and the periplasmic proteins AmeB and AmeC, suggesting an export channel into the environment similar to HAE1-type RND exporters. Proteins AmeABCD are encoded within a genetic island involved in the metabolism of acyclic and cyclic monoterpenes. The deletion of ameABCD translated into a decrease in tolerance to monoterpenes in liquid cultures. The addition of acetate as cosubstrate in limonene-containing cultures partially alleviated monoterpene toxicity in the deletion mutant. Accumulation of Nile Red in cells of C. defragrans required dissipation of the proton motive force with carbonyl cyanide m-chlorophenylhydrazone (CCCP). Cells lacking AmeABCD accumulated more Nile Red, suggesting an export function of the proteins. Our observations suggest that the tetrapartite RND transporter AmeABCD acts as an exporter during monoterpene detoxification in C. defragrans.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Puentes-Cala</LastName><ForeName>Edinson</ForeName><Initials>E</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-0587-2177</Identifier><AffiliationInfo><Affiliation>Dept. of Microbiology, Max Planck-Institute for Marine Microbiology, Celsiusstr. 1, 28359, Bremen, Germany. epuentes@mpi-bremen.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harder</LastName><ForeName>Jens</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Dept. of Microbiology, Max Planck-Institute for Marine Microbiology, Celsiusstr. 1, 28359, Bremen, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>10</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biodegradation</MedlineTA><NlmUniqueID>9100834</NlmUniqueID><ISSNLinking>0923-9820</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026901">Membrane Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D039821">Monoterpenes</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003198" MajorTopicYN="N">Computer Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016013" MajorTopicYN="N">Likelihood Functions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D026901" MajorTopicYN="N">Membrane Transport Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D039821" MajorTopicYN="N">Monoterpenes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005810" MajorTopicYN="N">Multigene Family</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020560" MajorTopicYN="N">Proteobacteria</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Anaerobic metabolism</Keyword><Keyword MajorTopicYN="Y">Castellaniella defragrans</Keyword><Keyword MajorTopicYN="Y">Monoterpene</Keyword><Keyword MajorTopicYN="Y">RND efflux pump</Keyword><Keyword MajorTopicYN="Y">Toxicity</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>05</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>09</Month><Day>27</Day></PubMedPubDate><PubMedPubDate 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