Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i<

Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insert...
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Autor*in:	Myriam Roth [verfasserIn] Emily C. A. Goodall [verfasserIn] Karthik Pullela [verfasserIn] Vincent Jaquet [verfasserIn] Patrice François [verfasserIn] Ian R. Henderson [verfasserIn] Karl-Heinz Krause [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	H TraDIS Tn-seq phophoglycerate mutase

Übergeordnetes Werk:	In: Antioxidants - MDPI AG, 2013, 11(2022), 10, p 2053
Übergeordnetes Werk:	volume:11 ; year:2022 ; number:10, p 2053

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/antiox11102053

Katalog-ID:	DOAJ083689354

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520			\|a Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<.
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allfields	10.3390/antiox11102053 doi (DE-627)DOAJ083689354 (DE-599)DOAJe8d29753612b459dbe5e7dadb85bf4a3 DE-627 ger DE-627 rakwb eng RM1-950 Myriam Roth verfasserin aut Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i< 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<. <i<E. coli</i< H<sub<2</sub<O<sub<2</sub< TraDIS Tn-seq phophoglycerate mutase <i<gpmA</i< Therapeutics. Pharmacology Emily C. A. Goodall verfasserin aut Karthik Pullela verfasserin aut Vincent Jaquet verfasserin aut Patrice François verfasserin aut Ian R. Henderson verfasserin aut Karl-Heinz Krause verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 2053 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 2053 https://doi.org/10.3390/antiox11102053 kostenfrei https://doaj.org/article/e8d29753612b459dbe5e7dadb85bf4a3 kostenfrei https://www.mdpi.com/2076-3921/11/10/2053 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 2053
spelling	10.3390/antiox11102053 doi (DE-627)DOAJ083689354 (DE-599)DOAJe8d29753612b459dbe5e7dadb85bf4a3 DE-627 ger DE-627 rakwb eng RM1-950 Myriam Roth verfasserin aut Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i< 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<. <i<E. coli</i< H<sub<2</sub<O<sub<2</sub< TraDIS Tn-seq phophoglycerate mutase <i<gpmA</i< Therapeutics. Pharmacology Emily C. A. Goodall verfasserin aut Karthik Pullela verfasserin aut Vincent Jaquet verfasserin aut Patrice François verfasserin aut Ian R. Henderson verfasserin aut Karl-Heinz Krause verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 2053 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 2053 https://doi.org/10.3390/antiox11102053 kostenfrei https://doaj.org/article/e8d29753612b459dbe5e7dadb85bf4a3 kostenfrei https://www.mdpi.com/2076-3921/11/10/2053 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 2053
allfields_unstemmed	10.3390/antiox11102053 doi (DE-627)DOAJ083689354 (DE-599)DOAJe8d29753612b459dbe5e7dadb85bf4a3 DE-627 ger DE-627 rakwb eng RM1-950 Myriam Roth verfasserin aut Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i< 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<. <i<E. coli</i< H<sub<2</sub<O<sub<2</sub< TraDIS Tn-seq phophoglycerate mutase <i<gpmA</i< Therapeutics. Pharmacology Emily C. A. Goodall verfasserin aut Karthik Pullela verfasserin aut Vincent Jaquet verfasserin aut Patrice François verfasserin aut Ian R. Henderson verfasserin aut Karl-Heinz Krause verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 2053 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 2053 https://doi.org/10.3390/antiox11102053 kostenfrei https://doaj.org/article/e8d29753612b459dbe5e7dadb85bf4a3 kostenfrei https://www.mdpi.com/2076-3921/11/10/2053 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 2053
allfieldsGer	10.3390/antiox11102053 doi (DE-627)DOAJ083689354 (DE-599)DOAJe8d29753612b459dbe5e7dadb85bf4a3 DE-627 ger DE-627 rakwb eng RM1-950 Myriam Roth verfasserin aut Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i< 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<. <i<E. coli</i< H<sub<2</sub<O<sub<2</sub< TraDIS Tn-seq phophoglycerate mutase <i<gpmA</i< Therapeutics. Pharmacology Emily C. A. Goodall verfasserin aut Karthik Pullela verfasserin aut Vincent Jaquet verfasserin aut Patrice François verfasserin aut Ian R. Henderson verfasserin aut Karl-Heinz Krause verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 2053 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 2053 https://doi.org/10.3390/antiox11102053 kostenfrei https://doaj.org/article/e8d29753612b459dbe5e7dadb85bf4a3 kostenfrei https://www.mdpi.com/2076-3921/11/10/2053 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 2053
allfieldsSound	10.3390/antiox11102053 doi (DE-627)DOAJ083689354 (DE-599)DOAJe8d29753612b459dbe5e7dadb85bf4a3 DE-627 ger DE-627 rakwb eng RM1-950 Myriam Roth verfasserin aut Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i< 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<. <i<E. coli</i< H<sub<2</sub<O<sub<2</sub< TraDIS Tn-seq phophoglycerate mutase <i<gpmA</i< Therapeutics. Pharmacology Emily C. A. Goodall verfasserin aut Karthik Pullela verfasserin aut Vincent Jaquet verfasserin aut Patrice François verfasserin aut Ian R. Henderson verfasserin aut Karl-Heinz Krause verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 2053 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 2053 https://doi.org/10.3390/antiox11102053 kostenfrei https://doaj.org/article/e8d29753612b459dbe5e7dadb85bf4a3 kostenfrei https://www.mdpi.com/2076-3921/11/10/2053 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 2053
language	English
source	In Antioxidants 11(2022), 10, p 2053 volume:11 year:2022 number:10, p 2053
sourceStr	In Antioxidants 11(2022), 10, p 2053 volume:11 year:2022 number:10, p 2053
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	<i<E. coli</i< H<sub<2</sub<O<sub<2</sub< TraDIS Tn-seq phophoglycerate mutase <i<gpmA</i< Therapeutics. Pharmacology
isfreeaccess_bool	true
container_title	Antioxidants
authorswithroles_txt_mv	Myriam Roth @@aut@@ Emily C. A. Goodall @@aut@@ Karthik Pullela @@aut@@ Vincent Jaquet @@aut@@ Patrice François @@aut@@ Ian R. Henderson @@aut@@ Karl-Heinz Krause @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	737287578
id	DOAJ083689354
language_de	englisch
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callnumber-first	R - Medicine
author	Myriam Roth
spellingShingle	Myriam Roth misc RM1-950 misc <i<E. coli</i< misc H<sub<2</sub<O<sub<2</sub< misc TraDIS misc Tn-seq misc phophoglycerate mutase misc <i<gpmA</i< misc Therapeutics. Pharmacology Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i<
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topic_title	RM1-950 Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i< <i<E. coli</i< H<sub<2</sub<O<sub<2</sub< TraDIS Tn-seq phophoglycerate mutase <i<gpmA</i<
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title	Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i<
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title_full	Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i<
author_sort	Myriam Roth
journal	Antioxidants
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author_browse	Myriam Roth Emily C. A. Goodall Karthik Pullela Vincent Jaquet Patrice François Ian R. Henderson Karl-Heinz Krause
container_volume	11
class	RM1-950
format_se	Elektronische Aufsätze
author-letter	Myriam Roth
doi_str_mv	10.3390/antiox11102053
author2-role	verfasserin
title_sort	transposon-directed insertion-site sequencing reveals glycolysis gene <i<gpma</i< as part of the h<sub<2</sub<o<sub<2</sub< defense mechanisms in <i<escherichia coli</i<
callnumber	RM1-950
title_auth	Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i<
abstract	Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<.
abstractGer	Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<.
abstract_unstemmed	Hydrogen peroxide (H<sub<2</sub<O<sub<2</sub<) is a common effector of defense mechanisms against pathogenic infections. However, bacterial factors involved in H<sub<2</sub<O<sub<2</sub< tolerance remain unclear. Here we used transposon-directed insertion-site sequencing (TraDIS), a technique allowing the screening of the whole genome, to identify genes implicated in H<sub<2</sub<O<sub<2</sub< tolerance in <i<Escherichia coli</i<. Our TraDIS analysis identified 10 mutants with fitness defect upon H<sub<2</sub<O<sub<2</sub< exposure, among which previously H<sub<2</sub<O<sub<2</sub<-associated genes (<i<oxyR</i<, <i<dps</i<, <i<dksA</i<, <i<rpoS</i<, <i<hfq</i< and <i<polA</i<) and other genes with no known association with H<sub<2</sub<O<sub<2</sub< tolerance in <i<E. coli</i< (<i<corA</i<, <i<rbsR</i<, <i<nhaA</i< and <i<gpmA</i<). This is the first description of the impact of <i<gpmA</i<, a gene involved in glycolysis, on the susceptibility of <i<E. coli</i< to H<sub<2</sub<O<sub<2</sub<. Indeed, confirmatory experiments showed that the deletion of <i<gpmA</i< led to a specific hypersensitivity to H<sub<2</sub<O<sub<2</sub< comparable to the deletion of the major H<sub<2</sub<O<sub<2</sub< scavenger gene <i<katG</i<. This hypersensitivity was not due to an alteration of catalase function and was independent of the carbon source or the presence of oxygen. Transcription of <i<gpmA</i< was upregulated under H<sub<2</sub<O<sub<2</sub< exposure, highlighting its role under oxidative stress. In summary, our TraDIS approach identified <i<gpmA</i< as a member of the oxidative stress defense mechanism in <i<E. coli</i<.
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container_issue	10, p 2053
title_short	Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i<
url	https://doi.org/10.3390/antiox11102053 https://doaj.org/article/e8d29753612b459dbe5e7dadb85bf4a3 https://www.mdpi.com/2076-3921/11/10/2053 https://doaj.org/toc/2076-3921
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author2	Emily C. A. Goodall Karthik Pullela Vincent Jaquet Patrice François Ian R. Henderson Karl-Heinz Krause
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up_date	2024-07-03T18:53:26.335Z
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Transposon-Directed Insertion-Site Sequencing Reveals Glycolysis Gene <i<gpmA</i< as Part of the H<sub<2</sub<O<sub<2</sub< Defense Mechanisms in <i<Escherichia coli</i<

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