SufT is required for growth of Mycobacterium smegmatis under iron limiting conditions.
Identifieur interne : 000029 ( Main/Exploration ); précédent : 000028; suivant : 000030SufT is required for growth of Mycobacterium smegmatis under iron limiting conditions.
Auteurs : Tsaone Tamuhla [Afrique du Sud] ; Lydia Joubert [États-Unis, Afrique du Sud] ; Danicke Willemse [États-Unis, Afrique du Sud] ; Monique J. Williams [Afrique du Sud]Source :
- Microbiology (Reading, England) [ 1465-2080 ] ; 2020.
Descripteurs français
- KwdFr :
- Aconitate hydratase (métabolisme), Biofilms (MeSH), Coenzymes (génétique), Délétion de gène (MeSH), Fer (métabolisme), Ferrosulfoprotéines (biosynthèse), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Mycobacterium smegmatis (génétique), Mycobacterium smegmatis (métabolisme), Protéines bactériennes (génétique), Succinate Dehydrogenase (métabolisme).
- MESH :
- biosynthèse : Ferrosulfoprotéines.
- génétique : Coenzymes, Ferrosulfoprotéines, Mycobacterium smegmatis, Protéines bactériennes.
- métabolisme : Aconitate hydratase, Fer, Ferrosulfoprotéines, Mycobacterium smegmatis, Succinate Dehydrogenase.
- Biofilms, Délétion de gène.
English descriptors
- KwdEn :
- Aconitate Hydratase (metabolism), Bacterial Proteins (genetics), Biofilms (MeSH), Coenzymes (genetics), Gene Deletion (MeSH), Iron (metabolism), Iron-Sulfur Proteins (biosynthesis), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Mycobacterium smegmatis (genetics), Mycobacterium smegmatis (metabolism), Succinate Dehydrogenase (metabolism).
- MESH :
- chemical , biosynthesis : Iron-Sulfur Proteins.
- chemical , genetics : Bacterial Proteins, Coenzymes, Iron-Sulfur Proteins.
- chemical , metabolism : Aconitate Hydratase, Iron, Iron-Sulfur Proteins, Succinate Dehydrogenase.
- genetics : Mycobacterium smegmatis.
- metabolism : Mycobacterium smegmatis.
- Biofilms, Gene Deletion.
Abstract
Iron-sulphur (FeS) clusters are versatile cofactors required for a range of biological processes within cells. Due to the reactive nature of the constituent molecules, assembly and delivery of these cofactors requires a multi-protein machinery in vivo. In prokaryotes, SufT homologues are proposed to function in the maturation and transfer of FeS clusters to apo-proteins. This study used targeted gene deletion to investigate the role of SufT in the physiology of mycobacteria, using Mycobacterium smegmatis as a model organism. Deletion of the sufT gene in M. smegmatis had no impact on growth under standard culture conditions and did not significantly alter activity of the FeS cluster dependent enzymes succinate dehydrogenase (SDH) and aconitase (ACN). Furthermore, the ΔsufT mutant was no more sensitive than the wild-type strain to the redox cycler 2,3-dimethoxy-1,4-naphthoquinone (DMNQ), or the anti-tuberculosis drugs isoniazid, clofazimine or rifampicin. In contrast, the ΔsufT mutant displayed a growth defect under iron limiting conditions, and an increased requirement for iron during biofilm formation. This data suggests that SufT is an accessory factor in FeS cluster biogenesis in mycobacteria which is required under conditions of iron limitation.
DOI: 10.1099/mic.0.000881
PubMed: 31860439
Affiliations:
Links toward previous steps (curation, corpus...)
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Williams</name><affiliation wicri:level="1"><nlm:affiliation>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town</wicri:regionArea><wicri:noRegion>Cape Town</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Present address: Department of Molecular and Cell Biology, University of Cape Town, Cape Town, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>Present address: Department of Molecular and Cell Biology, University of Cape Town, Cape Town</wicri:regionArea><wicri:noRegion>Cape Town</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:31860439</idno><idno type="pmid">31860439</idno><idno type="doi">10.1099/mic.0.000881</idno><idno type="wicri:Area/Main/Corpus">000172</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000172</idno><idno type="wicri:Area/Main/Curation">000172</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000172</idno><idno type="wicri:Area/Main/Exploration">000172</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">SufT is required for growth of <i>Mycobacterium smegmatis</i> under iron limiting conditions.</title><author><name sortKey="Tamuhla, Tsaone" sort="Tamuhla, Tsaone" uniqKey="Tamuhla T" first="Tsaone" last="Tamuhla">Tsaone Tamuhla</name><affiliation wicri:level="1"><nlm:affiliation>Present address: Department of Integrative Biomedical Sciences, Division of Computational Biology, Faculty of Health Sciences, University of Cape Town, Cape Town, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>Present address: Department of Integrative Biomedical Sciences, Division of Computational Biology, Faculty of Health Sciences, University of Cape Town, Cape Town</wicri:regionArea><wicri:noRegion>Cape Town</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town</wicri:regionArea><wicri:noRegion>Cape Town</wicri:noRegion></affiliation></author><author><name sortKey="Joubert, Lydia" sort="Joubert, Lydia" uniqKey="Joubert L" first="Lydia" last="Joubert">Lydia Joubert</name><affiliation wicri:level="1"><nlm:affiliation>Present address: Stanford-SLAC Cryo-EM Center, Stanford University, Stanford, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Present address: Stanford-SLAC Cryo-EM Center, Stanford University, Stanford</wicri:regionArea><wicri:noRegion>Stanford</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Central Analytical Facilties, Microbiology Department, Stellenbosch University, Stellenbosch, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>Central Analytical Facilties, Microbiology Department, Stellenbosch University, Stellenbosch</wicri:regionArea><wicri:noRegion>Stellenbosch</wicri:noRegion></affiliation></author><author><name sortKey="Willemse, Danicke" sort="Willemse, Danicke" uniqKey="Willemse D" first="Danicke" last="Willemse">Danicke Willemse</name><affiliation wicri:level="2"><nlm:affiliation>Present address: Texas Biomedical Research Institute, 8715 West Military Drive, San Antonio, TX, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Present address: Texas Biomedical Research Institute, 8715 West Military Drive, San Antonio, TX</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation><affiliation wicri:level="1"><nlm:affiliation>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town</wicri:regionArea><wicri:noRegion>Cape Town</wicri:noRegion></affiliation></author><author><name sortKey="Williams, Monique J" sort="Williams, Monique J" uniqKey="Williams M" first="Monique J" last="Williams">Monique J. Williams</name><affiliation wicri:level="1"><nlm:affiliation>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town</wicri:regionArea><wicri:noRegion>Cape Town</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Present address: Department of Molecular and Cell Biology, University of Cape Town, Cape Town, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>Present address: Department of Molecular and Cell Biology, University of Cape Town, Cape Town</wicri:regionArea><wicri:noRegion>Cape Town</wicri:noRegion></affiliation></author></analytic><series><title level="j">Microbiology (Reading, England)</title><idno type="eISSN">1465-2080</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aconitate Hydratase (metabolism)</term><term>Bacterial Proteins (genetics)</term><term>Biofilms (MeSH)</term><term>Coenzymes (genetics)</term><term>Gene Deletion (MeSH)</term><term>Iron (metabolism)</term><term>Iron-Sulfur Proteins (biosynthesis)</term><term>Iron-Sulfur Proteins (genetics)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Mycobacterium smegmatis (genetics)</term><term>Mycobacterium smegmatis (metabolism)</term><term>Succinate Dehydrogenase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aconitate hydratase (métabolisme)</term><term>Biofilms (MeSH)</term><term>Coenzymes (génétique)</term><term>Délétion de gène (MeSH)</term><term>Fer (métabolisme)</term><term>Ferrosulfoprotéines (biosynthèse)</term><term>Ferrosulfoprotéines (génétique)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Mycobacterium smegmatis (génétique)</term><term>Mycobacterium smegmatis (métabolisme)</term><term>Protéines bactériennes (génétique)</term><term>Succinate Dehydrogenase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Coenzymes</term><term>Iron-Sulfur Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aconitate Hydratase</term><term>Iron</term><term>Iron-Sulfur Proteins</term><term>Succinate Dehydrogenase</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Ferrosulfoprotéines</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mycobacterium smegmatis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Coenzymes</term><term>Ferrosulfoprotéines</term><term>Mycobacterium smegmatis</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mycobacterium smegmatis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aconitate hydratase</term><term>Fer</term><term>Ferrosulfoprotéines</term><term>Mycobacterium smegmatis</term><term>Succinate Dehydrogenase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biofilms</term><term>Gene Deletion</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biofilms</term><term>Délétion de gène</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Iron-sulphur (FeS) clusters are versatile cofactors required for a range of biological processes within cells. Due to the reactive nature of the constituent molecules, assembly and delivery of these cofactors requires a multi-protein machinery <i>in vivo</i>. In prokaryotes, SufT homologues are proposed to function in the maturation and transfer of FeS clusters to apo-proteins. This study used targeted gene deletion to investigate the role of SufT in the physiology of mycobacteria, using <i>Mycobacterium smegmatis</i> as a model organism. Deletion of the <i>sufT</i> gene in <i>M. smegmatis</i> had no impact on growth under standard culture conditions and did not significantly alter activity of the FeS cluster dependent enzymes succinate dehydrogenase (SDH) and aconitase (ACN). Furthermore, the Δ<i>sufT</i> mutant was no more sensitive than the wild-type strain to the redox cycler 2,3-dimethoxy-1,4-naphthoquinone (DMNQ), or the anti-tuberculosis drugs isoniazid, clofazimine or rifampicin. In contrast, the Δ<i>sufT</i> mutant displayed a growth defect under iron limiting conditions, and an increased requirement for iron during biofilm formation. This data suggests that SufT is an accessory factor in FeS cluster biogenesis in mycobacteria which is required under conditions of iron limitation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31860439</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>19</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1465-2080</ISSN><JournalIssue CitedMedium="Internet"><Volume>166</Volume><Issue>3</Issue><PubDate><Year>2020</Year><Month>03</Month></PubDate></JournalIssue><Title>Microbiology (Reading, England)</Title><ISOAbbreviation>Microbiology (Reading)</ISOAbbreviation></Journal><ArticleTitle>SufT is required for growth of <i>Mycobacterium smegmatis</i> under iron limiting conditions.</ArticleTitle><Pagination><MedlinePgn>296-305</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1099/mic.0.000881</ELocationID><Abstract><AbstractText>Iron-sulphur (FeS) clusters are versatile cofactors required for a range of biological processes within cells. Due to the reactive nature of the constituent molecules, assembly and delivery of these cofactors requires a multi-protein machinery <i>in vivo</i>. In prokaryotes, SufT homologues are proposed to function in the maturation and transfer of FeS clusters to apo-proteins. This study used targeted gene deletion to investigate the role of SufT in the physiology of mycobacteria, using <i>Mycobacterium smegmatis</i> as a model organism. Deletion of the <i>sufT</i> gene in <i>M. smegmatis</i> had no impact on growth under standard culture conditions and did not significantly alter activity of the FeS cluster dependent enzymes succinate dehydrogenase (SDH) and aconitase (ACN). Furthermore, the Δ<i>sufT</i> mutant was no more sensitive than the wild-type strain to the redox cycler 2,3-dimethoxy-1,4-naphthoquinone (DMNQ), or the anti-tuberculosis drugs isoniazid, clofazimine or rifampicin. In contrast, the Δ<i>sufT</i> mutant displayed a growth defect under iron limiting conditions, and an increased requirement for iron during biofilm formation. This data suggests that SufT is an accessory factor in FeS cluster biogenesis in mycobacteria which is required under conditions of iron limitation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tamuhla</LastName><ForeName>Tsaone</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Present address: Department of Integrative Biomedical Sciences, Division of Computational Biology, Faculty of Health Sciences, University of Cape Town, Cape Town, South Africa.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Joubert</LastName><ForeName>Lydia</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Present address: Stanford-SLAC Cryo-EM Center, Stanford University, Stanford, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Central Analytical Facilties, Microbiology Department, Stellenbosch University, Stellenbosch, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Willemse</LastName><ForeName>Danicke</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Present address: Texas Biomedical Research Institute, 8715 West Military Drive, San Antonio, TX, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Williams</LastName><ForeName>Monique J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>DST-NRF Centre of Excellence for Biomedical Tuberculosis Research; South African Medical Research Council Centre for Tuberculosis Research; Division of Molecular Biology and Human Genetics, Faculty of Medicine and Health Sciences, Stellenbosch University, Cape Town, South Africa.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Present address: Department of Molecular and Cell Biology, University of Cape Town, Cape Town, South Africa.</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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Microbiology (Reading)</MedlineTA><NlmUniqueID>9430468</NlmUniqueID><ISSNLinking>1350-0872</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003067">Coenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.3.99.1</RegistryNumber><NameOfSubstance UI="D013385">Succinate Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.3</RegistryNumber><NameOfSubstance UI="D000154">Aconitate Hydratase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000154" MajorTopicYN="N">Aconitate Hydratase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018441" MajorTopicYN="N">Biofilms</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003067" MajorTopicYN="N">Coenzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020102" MajorTopicYN="Y">Mycobacterium smegmatis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013385" MajorTopicYN="N">Succinate Dehydrogenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">biofilm</Keyword><Keyword MajorTopicYN="Y">iron</Keyword><Keyword MajorTopicYN="Y">iron-sulphur cluster</Keyword><Keyword MajorTopicYN="Y">mycobacterium</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate 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Joubert</name><name sortKey="Tamuhla, Tsaone" sort="Tamuhla, Tsaone" uniqKey="Tamuhla T" first="Tsaone" last="Tamuhla">Tsaone Tamuhla</name><name sortKey="Willemse, Danicke" sort="Willemse, Danicke" uniqKey="Willemse D" first="Danicke" last="Willemse">Danicke Willemse</name><name sortKey="Williams, Monique J" sort="Williams, Monique J" uniqKey="Williams M" first="Monique J" last="Williams">Monique J. Williams</name><name sortKey="Williams, Monique J" sort="Williams, Monique J" uniqKey="Williams M" first="Monique J" last="Williams">Monique J. Williams</name></country><country name="États-Unis"><noRegion><name sortKey="Joubert, Lydia" sort="Joubert, Lydia" uniqKey="Joubert L" first="Lydia" last="Joubert">Lydia Joubert</name></noRegion><name sortKey="Willemse, Danicke" sort="Willemse, Danicke" uniqKey="Willemse D" first="Danicke" last="Willemse">Danicke Willemse</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= SufT is required for growth of Mycobacterium smegmatis under iron limiting conditions.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:31860439" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a IronSulferCluV1
| This area was generated with Dilib version V0.6.38. |  |