Mercury resistance and mercuric reductase activities and expression among chemotrophic thermophilic Aquificae.
Identifieur interne : 001994 ( Main/Exploration ); précédent : 001993; suivant : 001995Mercury resistance and mercuric reductase activities and expression among chemotrophic thermophilic Aquificae.
Auteurs : Zachary Freedman [États-Unis] ; Chengsheng Zhu ; Tamar BarkaySource :
- Applied and environmental microbiology [ 1098-5336 ] ; 2012.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Analyse de profil d'expression de gènes (MeSH), Bactéries (croissance et développement), Bactéries (effets des médicaments et des substances chimiques), Bactéries (enzymologie), Bactéries (métabolisme), Données de séquences moléculaires (MeSH), Mercure (métabolisme), Mercure (toxicité), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Résistance bactérienne aux médicaments (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Température (MeSH).
- MESH :
- croissance et développement : Bactéries.
- effets des médicaments et des substances chimiques : Bactéries.
- enzymologie : Bactéries.
- métabolisme : Bactéries, Mercure, Oxidoreductases.
- toxicité : Mercure.
- Alignement de séquences, Analyse de profil d'expression de gènes, Données de séquences moléculaires, Oxydoréduction, Résistance bactérienne aux médicaments, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Température.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacteria (drug effects), Bacteria (enzymology), Bacteria (growth & development), Bacteria (metabolism), Drug Resistance, Bacterial (MeSH), Gene Expression Profiling (MeSH), Mercury (metabolism), Mercury (toxicity), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Temperature (MeSH).
- MESH :
- chemical , metabolism : Mercury, Oxidoreductases.
- drug effects : Bacteria.
- enzymology : Bacteria.
- growth & development : Bacteria.
- metabolism : Bacteria.
- chemical , toxicity : Mercury.
- Amino Acid Sequence, Drug Resistance, Bacterial, Gene Expression Profiling, Molecular Sequence Data, Oxidation-Reduction, Sequence Alignment, Sequence Homology, Amino Acid, Temperature.
Abstract
Mercury (Hg) resistance (mer) by the reduction of mercuric to elemental Hg is broadly distributed among the Bacteria and Archaea and plays an important role in Hg detoxification and biogeochemical cycling. MerA is the protein subunit of the homodimeric mercuric reductase (MR) enzyme, the central function of the mer system. MerA sequences in the phylum Aquificae form the deepest-branching lineage in Bayesian phylogenetic reconstructions of all known MerA homologs. We therefore hypothesized that the merA homologs in two thermophilic Aquificae, Hydrogenobaculum sp. strain Y04AAS1 (AAS1) and Hydrogenivirga sp. strain 128-5-R1-1 (R1-1), specified Hg resistance. Results supported this hypothesis, because strains AAS1 and R1-1 (i) were resistant to >10 μM Hg(II), (ii) transformed Hg(II) to Hg(0) during cellular growth, and (iii) possessed Hg-dependent NAD(P)H oxidation activities in crude cell extracts that were optimal at temperatures corresponding with the strains' optimal growth temperatures, 55°C for AAS1 and 70°C for R1-1. While these characteristics all conformed with the mer system paradigm, expression of the Aquificae mer operons was not induced by exposure to Hg(II) as indicated by unity ratios of merA transcripts, normalized to gyrA transcripts for hydrogen-grown AAS1 cultures, and by similar MR specific activities in thiosulfate-grown cultures with and without Hg(II). The Hg(II)-independent expression of mer in the deepest-branching lineage of MerA from bacteria whose natural habitats are Hg-rich geothermal environments suggests that regulated expression of mer was a later innovation likely in environments where microorganisms were intermittently exposed to toxic concentrations of Hg.
DOI: 10.1128/AEM.01060-12
PubMed: 22773655
PubMed Central: PMC3426723
Affiliations:
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uniqKey="Freedman Z" first="Zachary" last="Freedman">Zachary Freedman</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry and Microbiology, Rutgers University, New Brunswick, New Jersey, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Microbiology, Rutgers University, New Brunswick, New Jersey</wicri:regionArea><placeName><region type="state">New Jersey</region><settlement type="city">New Brunswick (New Jersey)</settlement></placeName><orgName type="university">Université Rutgers</orgName></affiliation></author><author><name sortKey="Zhu, Chengsheng" sort="Zhu, Chengsheng" uniqKey="Zhu C" first="Chengsheng" last="Zhu">Chengsheng Zhu</name></author><author><name sortKey="Barkay, Tamar" sort="Barkay, Tamar" uniqKey="Barkay T" first="Tamar" last="Barkay">Tamar Barkay</name></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno 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développement)</term><term>Bactéries (effets des médicaments et des substances chimiques)</term><term>Bactéries (enzymologie)</term><term>Bactéries (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Mercure (métabolisme)</term><term>Mercure (toxicité)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Résistance bactérienne aux médicaments (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Température (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Mercury</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Bactéries</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Bacteria</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Bactéries</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bactéries</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacteria</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Bacteria</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacteria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bactéries</term><term>Mercure</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Mercury</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Mercure</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Drug Resistance, Bacterial</term><term>Gene Expression Profiling</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Analyse de profil d'expression de gènes</term><term>Données de séquences moléculaires</term><term>Oxydoréduction</term><term>Résistance bactérienne aux médicaments</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mercury (Hg) resistance (mer) by the reduction of mercuric to elemental Hg is broadly distributed among the Bacteria and Archaea and plays an important role in Hg detoxification and biogeochemical cycling. MerA is the protein subunit of the homodimeric mercuric reductase (MR) enzyme, the central function of the mer system. MerA sequences in the phylum Aquificae form the deepest-branching lineage in Bayesian phylogenetic reconstructions of all known MerA homologs. We therefore hypothesized that the merA homologs in two thermophilic Aquificae, Hydrogenobaculum sp. strain Y04AAS1 (AAS1) and Hydrogenivirga sp. strain 128-5-R1-1 (R1-1), specified Hg resistance. Results supported this hypothesis, because strains AAS1 and R1-1 (i) were resistant to >10 μM Hg(II), (ii) transformed Hg(II) to Hg(0) during cellular growth, and (iii) possessed Hg-dependent NAD(P)H oxidation activities in crude cell extracts that were optimal at temperatures corresponding with the strains' optimal growth temperatures, 55°C for AAS1 and 70°C for R1-1. While these characteristics all conformed with the mer system paradigm, expression of the Aquificae mer operons was not induced by exposure to Hg(II) as indicated by unity ratios of merA transcripts, normalized to gyrA transcripts for hydrogen-grown AAS1 cultures, and by similar MR specific activities in thiosulfate-grown cultures with and without Hg(II). The Hg(II)-independent expression of mer in the deepest-branching lineage of MerA from bacteria whose natural habitats are Hg-rich geothermal environments suggests that regulated expression of mer was a later innovation likely in environments where microorganisms were intermittently exposed to toxic concentrations of Hg.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22773655</PMID><DateCompleted><Year>2012</Year><Month>12</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5336</ISSN><JournalIssue CitedMedium="Internet"><Volume>78</Volume><Issue>18</Issue><PubDate><Year>2012</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Mercury resistance and mercuric reductase activities and expression among chemotrophic thermophilic Aquificae.</ArticleTitle><Pagination><MedlinePgn>6568-75</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/AEM.01060-12</ELocationID><Abstract><AbstractText>Mercury (Hg) resistance (mer) by the reduction of mercuric to elemental Hg is broadly distributed among the Bacteria and Archaea and plays an important role in Hg detoxification and biogeochemical cycling. MerA is the protein subunit of the homodimeric mercuric reductase (MR) enzyme, the central function of the mer system. MerA sequences in the phylum Aquificae form the deepest-branching lineage in Bayesian phylogenetic reconstructions of all known MerA homologs. We therefore hypothesized that the merA homologs in two thermophilic Aquificae, Hydrogenobaculum sp. strain Y04AAS1 (AAS1) and Hydrogenivirga sp. strain 128-5-R1-1 (R1-1), specified Hg resistance. Results supported this hypothesis, because strains AAS1 and R1-1 (i) were resistant to >10 μM Hg(II), (ii) transformed Hg(II) to Hg(0) during cellular growth, and (iii) possessed Hg-dependent NAD(P)H oxidation activities in crude cell extracts that were optimal at temperatures corresponding with the strains' optimal growth temperatures, 55°C for AAS1 and 70°C for R1-1. While these characteristics all conformed with the mer system paradigm, expression of the Aquificae mer operons was not induced by exposure to Hg(II) as indicated by unity ratios of merA transcripts, normalized to gyrA transcripts for hydrogen-grown AAS1 cultures, and by similar MR specific activities in thiosulfate-grown cultures with and without Hg(II). The Hg(II)-independent expression of mer in the deepest-branching lineage of MerA from bacteria whose natural habitats are Hg-rich geothermal environments suggests that regulated expression of mer was a later innovation likely in environments where microorganisms were intermittently exposed to toxic concentrations of Hg.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Freedman</LastName><ForeName>Zachary</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Microbiology, Rutgers University, New Brunswick, New Jersey, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhu</LastName><ForeName>Chengsheng</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Barkay</LastName><ForeName>Tamar</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType 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sort="Zhu, Chengsheng" uniqKey="Zhu C" first="Chengsheng" last="Zhu">Chengsheng Zhu</name></noCountry><country name="États-Unis"><region name="New Jersey"><name sortKey="Freedman, Zachary" sort="Freedman, Zachary" uniqKey="Freedman Z" first="Zachary" last="Freedman">Zachary Freedman</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:22773655" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a DetoxFungiV1
| This area was generated with Dilib version V0.6.38. |  |