DetoxFungiV1, Main, Exploration, bibRecord, 001795

Identification of regions important for resistance and signalling within the antimicrobial peptide transporter BceAB of Bacillus subtilis.

Identifieur interne : 001795 ( Main/Exploration ); précédent : 001794; suivant : 001796

Identification of regions important for resistance and signalling within the antimicrobial peptide transporter BceAB of Bacillus subtilis.

Auteurs : Felix Kallenberg [Allemagne] ; Sebastian Dintner ; Roland Schmitz ; Susanne Gebhard

Source :

Journal of bacteriology [ 1098-5530 ] ; 2013.

RBID : pubmed:23687272

Descripteurs français

English descriptors

KwdEn :
- Anti-Bacterial Agents (metabolism), Antimicrobial Cationic Peptides (metabolism), Bacillus subtilis (genetics), Bacillus subtilis (metabolism), Bacitracin (metabolism), Bacteriocins (metabolism), Biological Transport, Active (MeSH), DNA Mutational Analysis (MeSH), Drug Resistance, Bacterial (MeSH), Gene Expression Regulation, Bacterial (MeSH), Membrane Transport Proteins (genetics), Membrane Transport Proteins (metabolism), Mutagenesis (MeSH), Peptides (metabolism), Protein Transport (MeSH), Signal Transduction (MeSH).
MESH :
- chemical , genetics : Membrane Transport Proteins.
- chemical , metabolism : Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacitracin, Bacteriocins, Membrane Transport Proteins, Peptides.
- genetics : Bacillus subtilis.
- metabolism : Bacillus subtilis.
- Biological Transport, Active, DNA Mutational Analysis, Drug Resistance, Bacterial, Gene Expression Regulation, Bacterial, Mutagenesis, Protein Transport, Signal Transduction.

Abstract

In the low-G+C-content Gram-positive bacteria, resistance to antimicrobial peptides is often mediated by so-called resistance modules. These consist of a two-component system and an ATP-binding cassette transporter and are characterized by an unusual mode of signal transduction where the transporter acts as a sensor of antimicrobial peptides, because the histidine kinase alone cannot detect the substrates directly. Thus, the transporters fulfill a dual function as sensors and detoxification systems to confer resistance, but the mechanistic details of these processes are unknown. The paradigm and best-understood example for this is the BceRS-BceAB module of Bacillus subtilis, which mediates resistance to bacitracin, mersacidin, and actagardine. Using a random mutagenesis approach, we here show that mutations that affect specific functions of the transporter BceAB are primarily found in the C-terminal region of the permease, BceB, particularly in the eighth transmembrane helix. Further, we show that while signaling and resistance are functionally interconnected, several mutations could be identified that strongly affected one activity of the transporter but had only minor effects on the other. Thus, a partial genetic separation of the two properties could be achieved by single amino acid replacements, providing first insights into the signaling mechanism of these unusual modules.

DOI: 10.1128/JB.00419-13
PubMed: 23687272
PubMed Central: PMC3697649

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Bacillus subtilis (metabolism)</term>
<term>Bacitracin (metabolism)</term>
<term>Bacteriocins (metabolism)</term>
<term>Biological Transport, Active (MeSH)</term>
<term>DNA Mutational Analysis (MeSH)</term>
<term>Drug Resistance, Bacterial (MeSH)</term>
<term>Gene Expression Regulation, Bacterial (MeSH)</term>
<term>Membrane Transport Proteins (genetics)</term>
<term>Membrane Transport Proteins (metabolism)</term>
<term>Mutagenesis (MeSH)</term>
<term>Peptides (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de mutations d'ADN (MeSH)</term>
<term>Antibactériens (métabolisme)</term>
<term>Bacillus subtilis (génétique)</term>
<term>Bacillus subtilis (métabolisme)</term>
<term>Bacitracine (métabolisme)</term>
<term>Bactériocines (métabolisme)</term>
<term>Mutagenèse (MeSH)</term>
<term>Peptides (métabolisme)</term>
<term>Peptides antimicrobiens cationiques (métabolisme)</term>
<term>Protéines de transport membranaire (génétique)</term>
<term>Protéines de transport membranaire (métabolisme)</term>
<term>Régulation de l'expression des gènes bactériens (MeSH)</term>
<term>Résistance bactérienne aux médicaments (MeSH)</term>
<term>Transduction du signal (MeSH)</term>
<term>Transport biologique actif (MeSH)</term>
<term>Transport des protéines (MeSH)</term>
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<term>Antimicrobial Cationic Peptides</term>
<term>Bacitracin</term>
<term>Bacteriocins</term>
<term>Membrane Transport Proteins</term>
<term>Peptides</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Bacillus subtilis</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Bacillus subtilis</term>
<term>Protéines de transport membranaire</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacillus subtilis</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antibactériens</term>
<term>Bacillus subtilis</term>
<term>Bacitracine</term>
<term>Bactériocines</term>
<term>Peptides</term>
<term>Peptides antimicrobiens cationiques</term>
<term>Protéines de transport membranaire</term>
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<keywords scheme="MESH" xml:lang="en"><term>Biological Transport, Active</term>
<term>DNA Mutational Analysis</term>
<term>Drug Resistance, Bacterial</term>
<term>Gene Expression Regulation, Bacterial</term>
<term>Mutagenesis</term>
<term>Protein Transport</term>
<term>Signal Transduction</term>
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<term>Mutagenèse</term>
<term>Régulation de l'expression des gènes bactériens</term>
<term>Résistance bactérienne aux médicaments</term>
<term>Transduction du signal</term>
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<front><div type="abstract" xml:lang="en">In the low-G+C-content Gram-positive bacteria, resistance to antimicrobial peptides is often mediated by so-called resistance modules. These consist of a two-component system and an ATP-binding cassette transporter and are characterized by an unusual mode of signal transduction where the transporter acts as a sensor of antimicrobial peptides, because the histidine kinase alone cannot detect the substrates directly. Thus, the transporters fulfill a dual function as sensors and detoxification systems to confer resistance, but the mechanistic details of these processes are unknown. The paradigm and best-understood example for this is the BceRS-BceAB module of Bacillus subtilis, which mediates resistance to bacitracin, mersacidin, and actagardine. Using a random mutagenesis approach, we here show that mutations that affect specific functions of the transporter BceAB are primarily found in the C-terminal region of the permease, BceB, particularly in the eighth transmembrane helix. Further, we show that while signaling and resistance are functionally interconnected, several mutations could be identified that strongly affected one activity of the transporter but had only minor effects on the other. Thus, a partial genetic separation of the two properties could be achieved by single amino acid replacements, providing first insights into the signaling mechanism of these unusual modules. </div>
</front>
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<Abstract><AbstractText>In the low-G+C-content Gram-positive bacteria, resistance to antimicrobial peptides is often mediated by so-called resistance modules. These consist of a two-component system and an ATP-binding cassette transporter and are characterized by an unusual mode of signal transduction where the transporter acts as a sensor of antimicrobial peptides, because the histidine kinase alone cannot detect the substrates directly. Thus, the transporters fulfill a dual function as sensors and detoxification systems to confer resistance, but the mechanistic details of these processes are unknown. The paradigm and best-understood example for this is the BceRS-BceAB module of Bacillus subtilis, which mediates resistance to bacitracin, mersacidin, and actagardine. Using a random mutagenesis approach, we here show that mutations that affect specific functions of the transporter BceAB are primarily found in the C-terminal region of the permease, BceB, particularly in the eighth transmembrane helix. Further, we show that while signaling and resistance are functionally interconnected, several mutations could be identified that strongly affected one activity of the transporter but had only minor effects on the other. Thus, a partial genetic separation of the two properties could be achieved by single amino acid replacements, providing first insights into the signaling mechanism of these unusual modules. </AbstractText>
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<tree><noCountry><name sortKey="Dintner, Sebastian" sort="Dintner, Sebastian" uniqKey="Dintner S" first="Sebastian" last="Dintner">Sebastian Dintner</name>
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<name sortKey="Schmitz, Roland" sort="Schmitz, Roland" uniqKey="Schmitz R" first="Roland" last="Schmitz">Roland Schmitz</name>
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   |texte=   Identification of regions important for resistance and signalling within the antimicrobial peptide transporter BceAB of Bacillus subtilis.
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Identification of regions important for resistance and signalling within the antimicrobial peptide transporter BceAB of Bacillus subtilis.

Identification of regions important for resistance and signalling within the antimicrobial peptide transporter BceAB of Bacillus subtilis.

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