IronSulferCluV1, Main, Exploration, bibRecord, 000165

Cancer-associated mutations in the iron-sulfur domain of FANCJ affect G-quadruplex metabolism.

Identifieur interne : 000165 ( Main/Exploration ); précédent : 000164; suivant : 000166

Cancer-associated mutations in the iron-sulfur domain of FANCJ affect G-quadruplex metabolism.

Auteurs : Diana C. Odermatt [Suisse] ; Wei Ting C. Lee [États-Unis] ; Sebastian Wild [Suisse] ; Stanislaw K. Jozwiakowski [Suisse] ; Eli Rothenberg [États-Unis] ; Kerstin Gari [Suisse]

Source :

PLoS genetics [ 1553-7404 ] ; 2020.

RBID : pubmed:32542039

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Binding Sites (MeSH), Fanconi Anemia Complementation Group Proteins (chemistry), Fanconi Anemia Complementation Group Proteins (genetics), Fanconi Anemia Complementation Group Proteins (metabolism), G-Quadruplexes (MeSH), HeLa Cells (MeSH), Humans (MeSH), Mutation (MeSH), Protein Binding (MeSH), RNA Helicases (chemistry), RNA Helicases (genetics), RNA Helicases (metabolism), Sf9 Cells (MeSH), Spodoptera (MeSH).
MESH :
- chemical , chemistry : Fanconi Anemia Complementation Group Proteins, RNA Helicases.
- chemical , genetics : Fanconi Anemia Complementation Group Proteins, RNA Helicases.
- chemical , metabolism : Fanconi Anemia Complementation Group Proteins, RNA Helicases.
- Animals, Binding Sites, G-Quadruplexes, HeLa Cells, Humans, Mutation, Protein Binding, Sf9 Cells, Spodoptera.

Abstract

FANCJ/BRIP1 is an iron-sulfur (FeS) cluster-binding DNA helicase involved in DNA inter-strand cross-link (ICL) repair and G-quadruplex (G4) metabolism. Mutations in FANCJ are associated with Fanconi anemia and an increased risk for developing breast and ovarian cancer. Several cancer-associated mutations are located in the FeS domain of FANCJ, but how they affect FeS cluster binding and/or FANCJ activity has remained mostly unclear. Here we show that the FeS cluster is indispensable for FANCJ's ability to unwind DNA substrates in vitro and to provide cellular resistance to agents that induce ICLs. Moreover, we find that FANCJ requires an intact FeS cluster for its ability to unfold G4 structures on the DNA template in a primer extension assay with the lagging-strand DNA polymerase delta. Surprisingly, however, FANCJ variants that are unable to bind an FeS cluster and to unwind DNA in vitro can partially suppress the formation of replisome-associated G4 structures that we observe in a FANCJ knock-out cell line. This may suggest a partially retained cellular activity of FANCJ variants with alterations in the FeS domain. On the other hand, FANCJ knock-out cells expressing FeS cluster-deficient variants display a similar-enhanced-sensitivity towards pyridostatin (PDS) and CX-5461, two agents that stabilise G4 structures, as FANCJ knock-out cells. Mutations in FANCJ that abolish FeS cluster binding may hence be predictive of an increased cellular sensitivity towards G4-stabilising agents.

DOI: 10.1371/journal.pgen.1008740
PubMed: 32542039
PubMed Central: PMC7316351

Affiliations:

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

to stream Main, to step Corpus: 000079
to stream Main, to step Curation: 000079

Le document en format XML

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<term>Binding Sites (MeSH)</term>
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<term>Fanconi Anemia Complementation Group Proteins (genetics)</term>
<term>Fanconi Anemia Complementation Group Proteins (metabolism)</term>
<term>G-Quadruplexes (MeSH)</term>
<term>HeLa Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>RNA Helicases (chemistry)</term>
<term>RNA Helicases (genetics)</term>
<term>RNA Helicases (metabolism)</term>
<term>Sf9 Cells (MeSH)</term>
<term>Spodoptera (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Cellules HeLa (MeSH)</term>
<term>Cellules Sf9 (MeSH)</term>
<term>G-quadruplexes (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Protéines des groupes de complémentation de l'anémie de Fanconi (composition chimique)</term>
<term>Protéines des groupes de complémentation de l'anémie de Fanconi (génétique)</term>
<term>Protéines des groupes de complémentation de l'anémie de Fanconi (métabolisme)</term>
<term>RNA helicases (composition chimique)</term>
<term>RNA helicases (génétique)</term>
<term>RNA helicases (métabolisme)</term>
<term>Sites de fixation (MeSH)</term>
<term>Spodoptera (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fanconi Anemia Complementation Group Proteins</term>
<term>RNA Helicases</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fanconi Anemia Complementation Group Proteins</term>
<term>RNA Helicases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fanconi Anemia Complementation Group Proteins</term>
<term>RNA Helicases</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines des groupes de complémentation de l'anémie de Fanconi</term>
<term>RNA helicases</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines des groupes de complémentation de l'anémie de Fanconi</term>
<term>RNA helicases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines des groupes de complémentation de l'anémie de Fanconi</term>
<term>RNA helicases</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Binding Sites</term>
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<term>HeLa Cells</term>
<term>Humans</term>
<term>Mutation</term>
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<term>Sf9 Cells</term>
<term>Spodoptera</term>
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<term>Cellules Sf9</term>
<term>G-quadruplexes</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
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<front><div type="abstract" xml:lang="en">FANCJ/BRIP1 is an iron-sulfur (FeS) cluster-binding DNA helicase involved in DNA inter-strand cross-link (ICL) repair and G-quadruplex (G4) metabolism. Mutations in FANCJ are associated with Fanconi anemia and an increased risk for developing breast and ovarian cancer. Several cancer-associated mutations are located in the FeS domain of FANCJ, but how they affect FeS cluster binding and/or FANCJ activity has remained mostly unclear. Here we show that the FeS cluster is indispensable for FANCJ's ability to unwind DNA substrates in vitro and to provide cellular resistance to agents that induce ICLs. Moreover, we find that FANCJ requires an intact FeS cluster for its ability to unfold G4 structures on the DNA template in a primer extension assay with the lagging-strand DNA polymerase delta. Surprisingly, however, FANCJ variants that are unable to bind an FeS cluster and to unwind DNA in vitro can partially suppress the formation of replisome-associated G4 structures that we observe in a FANCJ knock-out cell line. This may suggest a partially retained cellular activity of FANCJ variants with alterations in the FeS domain. On the other hand, FANCJ knock-out cells expressing FeS cluster-deficient variants display a similar-enhanced-sensitivity towards pyridostatin (PDS) and CX-5461, two agents that stabilise G4 structures, as FANCJ knock-out cells. Mutations in FANCJ that abolish FeS cluster binding may hence be predictive of an increased cellular sensitivity towards G4-stabilising agents.</div>
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<Abstract><AbstractText>FANCJ/BRIP1 is an iron-sulfur (FeS) cluster-binding DNA helicase involved in DNA inter-strand cross-link (ICL) repair and G-quadruplex (G4) metabolism. Mutations in FANCJ are associated with Fanconi anemia and an increased risk for developing breast and ovarian cancer. Several cancer-associated mutations are located in the FeS domain of FANCJ, but how they affect FeS cluster binding and/or FANCJ activity has remained mostly unclear. Here we show that the FeS cluster is indispensable for FANCJ's ability to unwind DNA substrates in vitro and to provide cellular resistance to agents that induce ICLs. Moreover, we find that FANCJ requires an intact FeS cluster for its ability to unfold G4 structures on the DNA template in a primer extension assay with the lagging-strand DNA polymerase delta. Surprisingly, however, FANCJ variants that are unable to bind an FeS cluster and to unwind DNA in vitro can partially suppress the formation of replisome-associated G4 structures that we observe in a FANCJ knock-out cell line. This may suggest a partially retained cellular activity of FANCJ variants with alterations in the FeS domain. On the other hand, FANCJ knock-out cells expressing FeS cluster-deficient variants display a similar-enhanced-sensitivity towards pyridostatin (PDS) and CX-5461, two agents that stabilise G4 structures, as FANCJ knock-out cells. Mutations in FANCJ that abolish FeS cluster binding may hence be predictive of an increased cellular sensitivity towards G4-stabilising agents.</AbstractText>
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<CoiStatement>The authors have declared that no competing interests exist.</CoiStatement>
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Cancer-associated mutations in the iron-sulfur domain of FANCJ affect G-quadruplex metabolism.

Cancer-associated mutations in the iron-sulfur domain of FANCJ affect G-quadruplex metabolism.

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