GlutaredoxinV1, Main, Exploration, bibRecord, 000294

A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.

Identifieur interne : 000294 ( Main/Exploration ); précédent : 000293; suivant : 000295

A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.

Auteurs : Samantha Ebersoll [Allemagne] ; Blessing Musunda [Allemagne] ; Torsten Schmenger [Allemagne] ; Natalie Dirdjaja [Allemagne] ; Mariana Bonilla [Uruguay] ; Bruno Manta [Uruguay] ; Kathrin Ulrich [Allemagne] ; Marcelo A. Comini [Uruguay] ; R Luise Krauth-Siegel [Allemagne]

Source :

Redox biology [ 2213-2317 ] ; 2018.

RBID : pubmed:29413965

Descripteurs français

KwdFr :
- Adaptation physiologique (génétique), Adénosine triphosphate (métabolisme), Allèles (MeSH), Animaux (MeSH), Cytosol (métabolisme), Domaine catalytique (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Humains (MeSH), Maladie du sommeil (anatomopathologie), Maladie du sommeil (métabolisme), Maladie du sommeil (parasitologie), Membranes mitochondriales (métabolisme), Mitochondries (génétique), Mitochondries (métabolisme), Mitochondries (parasitologie), Mutation (MeSH), Oxydoréduction (MeSH), Prolifération cellulaire (génétique), Souris (MeSH), Température élevée (MeSH), Trypanosoma brucei brucei (métabolisme), Trypanosoma brucei brucei (pathogénicité).
MESH :
- anatomopathologie : Maladie du sommeil.
- composition chimique : Glutarédoxines.
- génétique : Adaptation physiologique, Glutarédoxines, Mitochondries, Prolifération cellulaire.
- métabolisme : Adénosine triphosphate, Cytosol, Glutarédoxines, Maladie du sommeil, Membranes mitochondriales, Mitochondries, Trypanosoma brucei brucei.
- parasitologie : Maladie du sommeil, Mitochondries.
- pathogénicité : Trypanosoma brucei brucei.
- Allèles, Animaux, Domaine catalytique, Humains, Mutation, Oxydoréduction, Souris, Température élevée.

English descriptors

KwdEn :
- Adaptation, Physiological (genetics), Adenosine Triphosphate (metabolism), Alleles (MeSH), Animals (MeSH), Catalytic Domain (MeSH), Cell Proliferation (genetics), Cytosol (metabolism), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Hot Temperature (MeSH), Humans (MeSH), Mice (MeSH), Mitochondria (genetics), Mitochondria (metabolism), Mitochondria (parasitology), Mitochondrial Membranes (metabolism), Mutation (MeSH), Oxidation-Reduction (MeSH), Trypanosoma brucei brucei (metabolism), Trypanosoma brucei brucei (pathogenicity), Trypanosomiasis, African (metabolism), Trypanosomiasis, African (parasitology), Trypanosomiasis, African (pathology).
MESH :
- chemical , chemistry : Glutaredoxins.
- chemical , genetics : Glutaredoxins.
- chemical , metabolism : Adenosine Triphosphate, Glutaredoxins.
- genetics : Adaptation, Physiological, Cell Proliferation, Mitochondria.
- metabolism : Cytosol, Mitochondria, Mitochondrial Membranes, Trypanosoma brucei brucei, Trypanosomiasis, African.
- parasitology : Mitochondria, Trypanosomiasis, African.
- pathogenicity : Trypanosoma brucei brucei.
- pathology : Trypanosomiasis, African.
- Alleles, Animals, Catalytic Domain, Hot Temperature, Humans, Mice, Mutation, Oxidation-Reduction.

Abstract

Trypanosoma brucei glutaredoxin 2 (Grx2) is a dithiol glutaredoxin that is specifically located in the mitochondrial intermembrane space. Bloodstream form parasites lacking Grx2 or both, Grx2 and the cytosolic Grx1, are viable in vitro and infectious to mice suggesting that neither oxidoreductase is needed for survival or infectivity to mammals. A 37 °C to 39 °C shift changes the cellular redox milieu of bloodstream cells to more oxidizing conditions and induces a significantly stronger growth arrest in wildtype parasites compared to the mutant cells. Grx2-deficient cells ectopically expressing the wildtype form of Grx2 with its C31QFC34 active site, but not the C34S mutant, regain the sensitivity of the parental strain, indicating that the physiological role of Grx2 requires both active site cysteines. In the procyclic insect stage of the parasite, Grx2 is essential. Both alleles can be replaced if procyclic cells ectopically express authentic or C34S, but not C31S/C34S Grx2, pointing to a redox role that relies on a monothiol mechanism. RNA-interference against Grx2 causes a virtually irreversible proliferation defect. The cells adopt an elongated morphology but do not show any significant alteration in the cell cycle. The growth retardation is attenuated by high glucose concentrations. Under these conditions, procyclic cells obtain ATP by substrate level phosphorylation suggesting that Grx2 might regulate a respiratory chain component.

DOI: 10.1016/j.redox.2018.01.011
PubMed: 29413965
PubMed Central: PMC5975080

Affiliations:

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

to stream Main, to step Corpus: 000265
to stream Main, to step Curation: 000265

Le document en format XML

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<term>Adenosine Triphosphate (metabolism)</term>
<term>Alleles (MeSH)</term>
<term>Animals (MeSH)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Cell Proliferation (genetics)</term>
<term>Cytosol (metabolism)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Hot Temperature (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Mitochondria (genetics)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondria (parasitology)</term>
<term>Mitochondrial Membranes (metabolism)</term>
<term>Mutation (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Trypanosoma brucei brucei (metabolism)</term>
<term>Trypanosoma brucei brucei (pathogenicity)</term>
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<term>Adénosine triphosphate (métabolisme)</term>
<term>Allèles (MeSH)</term>
<term>Animaux (MeSH)</term>
<term>Cytosol (métabolisme)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Maladie du sommeil (anatomopathologie)</term>
<term>Maladie du sommeil (métabolisme)</term>
<term>Maladie du sommeil (parasitologie)</term>
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<term>Mitochondries (métabolisme)</term>
<term>Mitochondries (parasitologie)</term>
<term>Mutation (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
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<term>Souris (MeSH)</term>
<term>Température élevée (MeSH)</term>
<term>Trypanosoma brucei brucei (métabolisme)</term>
<term>Trypanosoma brucei brucei (pathogénicité)</term>
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<term>Glutaredoxins</term>
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</keywords>
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</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Adaptation, Physiological</term>
<term>Cell Proliferation</term>
<term>Mitochondria</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Adaptation physiologique</term>
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<term>Mitochondries</term>
<term>Prolifération cellulaire</term>
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<term>Mitochondria</term>
<term>Mitochondrial Membranes</term>
<term>Trypanosoma brucei brucei</term>
<term>Trypanosomiasis, African</term>
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<term>Cytosol</term>
<term>Glutarédoxines</term>
<term>Maladie du sommeil</term>
<term>Membranes mitochondriales</term>
<term>Mitochondries</term>
<term>Trypanosoma brucei brucei</term>
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<keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Maladie du sommeil</term>
<term>Mitochondries</term>
</keywords>
<keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Mitochondria</term>
<term>Trypanosomiasis, African</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Trypanosoma brucei brucei</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Trypanosoma brucei brucei</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Trypanosomiasis, African</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Alleles</term>
<term>Animals</term>
<term>Catalytic Domain</term>
<term>Hot Temperature</term>
<term>Humans</term>
<term>Mice</term>
<term>Mutation</term>
<term>Oxidation-Reduction</term>
</keywords>
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<term>Animaux</term>
<term>Domaine catalytique</term>
<term>Humains</term>
<term>Mutation</term>
<term>Oxydoréduction</term>
<term>Souris</term>
<term>Température élevée</term>
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<front><div type="abstract" xml:lang="en">Trypanosoma brucei glutaredoxin 2 (Grx2) is a dithiol glutaredoxin that is specifically located in the mitochondrial intermembrane space. Bloodstream form parasites lacking Grx2 or both, Grx2 and the cytosolic Grx1, are viable in vitro and infectious to mice suggesting that neither oxidoreductase is needed for survival or infectivity to mammals. A 37 °C to 39 °C shift changes the cellular redox milieu of bloodstream cells to more oxidizing conditions and induces a significantly stronger growth arrest in wildtype parasites compared to the mutant cells. Grx2-deficient cells ectopically expressing the wildtype form of Grx2 with its C31QFC34 active site, but not the C34S mutant, regain the sensitivity of the parental strain, indicating that the physiological role of Grx2 requires both active site cysteines. In the procyclic insect stage of the parasite, Grx2 is essential. Both alleles can be replaced if procyclic cells ectopically express authentic or C34S, but not C31S/C34S Grx2, pointing to a redox role that relies on a monothiol mechanism. RNA-interference against Grx2 causes a virtually irreversible proliferation defect. The cells adopt an elongated morphology but do not show any significant alteration in the cell cycle. The growth retardation is attenuated by high glucose concentrations. Under these conditions, procyclic cells obtain ATP by substrate level phosphorylation suggesting that Grx2 might regulate a respiratory chain component.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29413965</PMID>
<DateCompleted><Year>2018</Year>
<Month>10</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2213-2317</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>15</Volume>
<PubDate><Year>2018</Year>
<Month>05</Month>
</PubDate>
</JournalIssue>
<Title>Redox biology</Title>
<ISOAbbreviation>Redox Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.</ArticleTitle>
<Pagination><MedlinePgn>532-547</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S2213-2317(17)30981-3</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.redox.2018.01.011</ELocationID>
<Abstract><AbstractText>Trypanosoma brucei glutaredoxin 2 (Grx2) is a dithiol glutaredoxin that is specifically located in the mitochondrial intermembrane space. Bloodstream form parasites lacking Grx2 or both, Grx2 and the cytosolic Grx1, are viable in vitro and infectious to mice suggesting that neither oxidoreductase is needed for survival or infectivity to mammals. A 37 °C to 39 °C shift changes the cellular redox milieu of bloodstream cells to more oxidizing conditions and induces a significantly stronger growth arrest in wildtype parasites compared to the mutant cells. Grx2-deficient cells ectopically expressing the wildtype form of Grx2 with its C31QFC34 active site, but not the C34S mutant, regain the sensitivity of the parental strain, indicating that the physiological role of Grx2 requires both active site cysteines. In the procyclic insect stage of the parasite, Grx2 is essential. Both alleles can be replaced if procyclic cells ectopically express authentic or C34S, but not C31S/C34S Grx2, pointing to a redox role that relies on a monothiol mechanism. RNA-interference against Grx2 causes a virtually irreversible proliferation defect. The cells adopt an elongated morphology but do not show any significant alteration in the cell cycle. The growth retardation is attenuated by high glucose concentrations. Under these conditions, procyclic cells obtain ATP by substrate level phosphorylation suggesting that Grx2 might regulate a respiratory chain component.</AbstractText>
<CopyrightInformation>Copyright © 2018 The Authors. Published by Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ebersoll</LastName>
<ForeName>Samantha</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Musunda</LastName>
<ForeName>Blessing</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Schmenger</LastName>
<ForeName>Torsten</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dirdjaja</LastName>
<ForeName>Natalie</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bonilla</LastName>
<ForeName>Mariana</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Group Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Manta</LastName>
<ForeName>Bruno</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Group Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Ulrich</LastName>
<ForeName>Kathrin</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Comini</LastName>
<ForeName>Marcelo A</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Group Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Krauth-Siegel</LastName>
<ForeName>R Luise</ForeName>
<Initials>RL</Initials>
<AffiliationInfo><Affiliation>Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. Electronic address: luise.krauth-siegel@bzh.uni-heidelberg.de.</Affiliation>
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<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<Month>01</Month>
<Day>31</Day>
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<NlmUniqueID>101605639</NlmUniqueID>
<ISSNLinking>2213-2317</ISSNLinking>
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<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
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<MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName>
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<MeshHeading><DescriptorName UI="D051336" MajorTopicYN="N">Mitochondrial Membranes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
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<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
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<Keyword MajorTopicYN="Y">Trypanothione</Keyword>
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<name sortKey="Krauth Siegel, R Luise" sort="Krauth Siegel, R Luise" uniqKey="Krauth Siegel R" first="R Luise" last="Krauth-Siegel">R Luise Krauth-Siegel</name>
<name sortKey="Musunda, Blessing" sort="Musunda, Blessing" uniqKey="Musunda B" first="Blessing" last="Musunda">Blessing Musunda</name>
<name sortKey="Schmenger, Torsten" sort="Schmenger, Torsten" uniqKey="Schmenger T" first="Torsten" last="Schmenger">Torsten Schmenger</name>
<name sortKey="Ulrich, Kathrin" sort="Ulrich, Kathrin" uniqKey="Ulrich K" first="Kathrin" last="Ulrich">Kathrin Ulrich</name>
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<country name="Uruguay"><noRegion><name sortKey="Bonilla, Mariana" sort="Bonilla, Mariana" uniqKey="Bonilla M" first="Mariana" last="Bonilla">Mariana Bonilla</name>
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<name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name>
<name sortKey="Manta, Bruno" sort="Manta, Bruno" uniqKey="Manta B" first="Bruno" last="Manta">Bruno Manta</name>
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Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000294 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000294 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:29413965
   |texte=   A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:29413965" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a GlutaredoxinV1

This area was generated with Dilib version V0.6.37.
Data generation: Wed Nov 18 15:13:42 2020. Site generation: Wed Nov 18 15:16:12 2020

	Serveur d'exploration sur la glutarédoxine
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la glutarédoxine

A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.

A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.

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Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki