GlutaredoxinV1, Main, Exploration, bibRecord, 000150

Mechanism of frataxin "bypass" in human iron-sulfur cluster biosynthesis with implications for Friedreich's ataxia.

Identifieur interne : 000150 ( Main/Exploration ); précédent : 000149; suivant : 000151

Mechanism of frataxin "bypass" in human iron-sulfur cluster biosynthesis with implications for Friedreich's ataxia.

Auteurs : Deepika Das [États-Unis] ; Shachin Patra [États-Unis] ; Jennifer Bridwell-Rabb [États-Unis] ; David P. Barondeau [États-Unis]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2019.

RBID : pubmed:30975898

Descripteurs français

KwdFr :
- Ataxie de Friedreich (anatomopathologie), Ataxie de Friedreich (métabolisme), Carbon-sulfur lyases (métabolisme), Cinétique (MeSH), Ferrosulfoprotéines (génétique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (métabolisme), Humains (MeSH), Liaison aux protéines (MeSH), Mutagenèse dirigée (MeSH), Protéines de liaison au fer (génétique), Protéines de liaison au fer (métabolisme), Régulation allostérique (MeSH).
MESH :
- anatomopathologie : Ataxie de Friedreich.
- génétique : Ferrosulfoprotéines, Protéines de liaison au fer.
- métabolisme : Ataxie de Friedreich, Carbon-sulfur lyases, Ferrosulfoprotéines, Glutarédoxines, Protéines de liaison au fer.
- Cinétique, Humains, Liaison aux protéines, Mutagenèse dirigée, Régulation allostérique.

English descriptors

KwdEn :
- Allosteric Regulation (MeSH), Carbon-Sulfur Lyases (metabolism), Friedreich Ataxia (metabolism), Friedreich Ataxia (pathology), Glutaredoxins (metabolism), Humans (MeSH), Iron-Binding Proteins (genetics), Iron-Binding Proteins (metabolism), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Kinetics (MeSH), Mutagenesis, Site-Directed (MeSH), Protein Binding (MeSH).
MESH :
- chemical , genetics : Iron-Binding Proteins, Iron-Sulfur Proteins.
- chemical , metabolism : Carbon-Sulfur Lyases, Glutaredoxins, Iron-Binding Proteins, Iron-Sulfur Proteins.
- metabolism : Friedreich Ataxia.
- pathology : Friedreich Ataxia.
- Allosteric Regulation, Humans, Kinetics, Mutagenesis, Site-Directed, Protein Binding.

Abstract

In humans, mitochondrial iron-sulfur cluster biosynthesis is an essential biochemical process mediated by the assembly complex consisting of cysteine desulfurase (NFS1), LYR protein (ISD11), acyl-carrier protein (ACP), and the iron-sulfur cluster assembly scaffold protein (ISCU2). The protein frataxin (FXN) is an allosteric activator that binds the assembly complex and stimulates the cysteine desulfurase and iron-sulfur cluster assembly activities. FXN depletion causes loss of activity of iron-sulfur-dependent enzymes and the development of the neurodegenerative disease Friedreich's ataxia. Recently, a mutation that suppressed the loss of the FXN homolog in Saccharomyces cerevisiae was identified that encodes an amino acid substitution equivalent to the human variant ISCU2 M140I. Here, we developed iron-sulfur cluster synthesis and transfer functional assays and determined that the human ISCU2 M140I variant can substitute for FXN in accelerating the rate of iron-sulfur cluster formation on the monothiol glutaredoxin (GRX5) acceptor protein. Incorporation of both FXN and the M140I substitution had an additive effect, suggesting an acceleration of distinct steps in iron-sulfur cluster biogenesis. In contrast to the canonical role of FXN in stimulating the formation of [2Fe-2S]-ISCU2 intermediates, we found here that the M140I substitution in ISCU2 promotes the transfer of iron-sulfur clusters to GRX5. Together, these results reveal an unexpected mechanism that replaces FXN-based stimulation of the iron-sulfur cluster biosynthetic pathway and suggest new strategies to overcome the loss of cellular FXN that may be relevant to the development of therapeutics for Friedreich's ataxia.

DOI: 10.1074/jbc.RA119.007716
PubMed: 30975898
PubMed Central: PMC6556584

Affiliations:

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Le document en format XML

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<series><title level="j">The Journal of biological chemistry</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation (MeSH)</term>
<term>Carbon-Sulfur Lyases (metabolism)</term>
<term>Friedreich Ataxia (metabolism)</term>
<term>Friedreich Ataxia (pathology)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Iron-Binding Proteins (genetics)</term>
<term>Iron-Binding Proteins (metabolism)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Protein Binding (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Ataxie de Friedreich (anatomopathologie)</term>
<term>Ataxie de Friedreich (métabolisme)</term>
<term>Carbon-sulfur lyases (métabolisme)</term>
<term>Cinétique (MeSH)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Protéines de liaison au fer (génétique)</term>
<term>Protéines de liaison au fer (métabolisme)</term>
<term>Régulation allostérique (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Iron-Binding Proteins</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbon-Sulfur Lyases</term>
<term>Glutaredoxins</term>
<term>Iron-Binding Proteins</term>
<term>Iron-Sulfur Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Ataxie de Friedreich</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferrosulfoprotéines</term>
<term>Protéines de liaison au fer</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Friedreich Ataxia</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ataxie de Friedreich</term>
<term>Carbon-sulfur lyases</term>
<term>Ferrosulfoprotéines</term>
<term>Glutarédoxines</term>
<term>Protéines de liaison au fer</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Friedreich Ataxia</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term>
<term>Humans</term>
<term>Kinetics</term>
<term>Mutagenesis, Site-Directed</term>
<term>Protein Binding</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Mutagenèse dirigée</term>
<term>Régulation allostérique</term>
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<front><div type="abstract" xml:lang="en">In humans, mitochondrial iron-sulfur cluster biosynthesis is an essential biochemical process mediated by the assembly complex consisting of cysteine desulfurase (NFS1), LYR protein (ISD11), acyl-carrier protein (ACP), and the iron-sulfur cluster assembly scaffold protein (ISCU2). The protein frataxin (FXN) is an allosteric activator that binds the assembly complex and stimulates the cysteine desulfurase and iron-sulfur cluster assembly activities. FXN depletion causes loss of activity of iron-sulfur-dependent enzymes and the development of the neurodegenerative disease Friedreich's ataxia. Recently, a mutation that suppressed the loss of the <i>FXN</i>
 homolog in <i>Saccharomyces cerevisiae</i>
 was identified that encodes an amino acid substitution equivalent to the human variant ISCU2 M140I. Here, we developed iron-sulfur cluster synthesis and transfer functional assays and determined that the human ISCU2 M140I variant can substitute for FXN in accelerating the rate of iron-sulfur cluster formation on the monothiol glutaredoxin (GRX5) acceptor protein. Incorporation of both FXN and the M140I substitution had an additive effect, suggesting an acceleration of distinct steps in iron-sulfur cluster biogenesis. In contrast to the canonical role of FXN in stimulating the formation of [2Fe-2S]-ISCU2 intermediates, we found here that the M140I substitution in ISCU2 promotes the transfer of iron-sulfur clusters to GRX5. Together, these results reveal an unexpected mechanism that replaces FXN-based stimulation of the iron-sulfur cluster biosynthetic pathway and suggest new strategies to overcome the loss of cellular FXN that may be relevant to the development of therapeutics for Friedreich's ataxia.</div>
</front>
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<Abstract><AbstractText>In humans, mitochondrial iron-sulfur cluster biosynthesis is an essential biochemical process mediated by the assembly complex consisting of cysteine desulfurase (NFS1), LYR protein (ISD11), acyl-carrier protein (ACP), and the iron-sulfur cluster assembly scaffold protein (ISCU2). The protein frataxin (FXN) is an allosteric activator that binds the assembly complex and stimulates the cysteine desulfurase and iron-sulfur cluster assembly activities. FXN depletion causes loss of activity of iron-sulfur-dependent enzymes and the development of the neurodegenerative disease Friedreich's ataxia. Recently, a mutation that suppressed the loss of the <i>FXN</i>
 homolog in <i>Saccharomyces cerevisiae</i>
 was identified that encodes an amino acid substitution equivalent to the human variant ISCU2 M140I. Here, we developed iron-sulfur cluster synthesis and transfer functional assays and determined that the human ISCU2 M140I variant can substitute for FXN in accelerating the rate of iron-sulfur cluster formation on the monothiol glutaredoxin (GRX5) acceptor protein. Incorporation of both FXN and the M140I substitution had an additive effect, suggesting an acceleration of distinct steps in iron-sulfur cluster biogenesis. In contrast to the canonical role of FXN in stimulating the formation of [2Fe-2S]-ISCU2 intermediates, we found here that the M140I substitution in ISCU2 promotes the transfer of iron-sulfur clusters to GRX5. Together, these results reveal an unexpected mechanism that replaces FXN-based stimulation of the iron-sulfur cluster biosynthetic pathway and suggest new strategies to overcome the loss of cellular FXN that may be relevant to the development of therapeutics for Friedreich's ataxia.</AbstractText>
<CopyrightInformation>© 2019 Das et al.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Das</LastName>
<ForeName>Deepika</ForeName>
<Initials>D</Initials>
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<ForeName>Shachin</ForeName>
<Initials>S</Initials>
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<AffiliationInfo><Affiliation>From the Department of Chemistry, Texas A & M University, College Station, Texas 77842.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Bridwell-Rabb</LastName>
<ForeName>Jennifer</ForeName>
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</AffiliationInfo>
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<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
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<MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
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</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">ISCU2 M140I</Keyword>
<Keyword MajorTopicYN="Y">analytical ultracentrifugation</Keyword>
<Keyword MajorTopicYN="Y">circular dichroism (CD)</Keyword>
<Keyword MajorTopicYN="Y">cysteine labeling</Keyword>
<Keyword MajorTopicYN="Y">enzyme kinetics</Keyword>
<Keyword MajorTopicYN="Y">fluorescence anisotropy</Keyword>
<Keyword MajorTopicYN="Y">iron–sulfur assembly</Keyword>
<Keyword MajorTopicYN="Y">iron–sulfur protein</Keyword>
<Keyword MajorTopicYN="Y">mitochondrial disease</Keyword>
<Keyword MajorTopicYN="Y">neurodegeneration</Keyword>
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Mechanism of frataxin "bypass" in human iron-sulfur cluster biosynthesis with implications for Friedreich's ataxia.

Mechanism of frataxin "bypass" in human iron-sulfur cluster biosynthesis with implications for Friedreich's ataxia.

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