GlutaredoxinV1, Main, Exploration, bibRecord, 000394

A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.

Identifieur interne : 000394 ( Main/Exploration ); précédent : 000393; suivant : 000395

A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.

Auteurs : Christoph Loderer [Suède] ; Venkateswara Rao Jonna [Suède] ; Mikael Crona [Suède] ; Inna Rozman Grinberg [Suède] ; Margareta Sahlin [Suède] ; Anders Hofer [Suède] ; Daniel Lundin [Suède] ; Britt-Marie Sjöberg [Suède]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2017.

RBID : pubmed:28972190

Descripteurs français

English descriptors

KwdEn :
- Actinomycetales (chemistry), Actinomycetales (genetics), Actinomycetales (metabolism), Allosteric Regulation (MeSH), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Catalytic Domain (MeSH), Crystallography, X-Ray (MeSH), Cysteine (chemistry), Cysteine (genetics), Cysteine (metabolism), Electron Transport (MeSH), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Phylogeny (MeSH), Protein Domains (MeSH), Protein Multimerization (MeSH), Ribonucleotide Reductases (chemistry), Ribonucleotide Reductases (genetics), Ribonucleotide Reductases (metabolism), Zinc Fingers (MeSH).
MESH :
- chemical , chemistry : Bacterial Proteins, Cysteine, Ribonucleotide Reductases.
- chemistry : Actinomycetales.
- genetics : Actinomycetales, Bacterial Proteins, Cysteine, Ribonucleotide Reductases.
- metabolism : Actinomycetales, Bacterial Proteins, Cysteine, Ribonucleotide Reductases.
- Allosteric Regulation, Catalytic Domain, Crystallography, X-Ray, Electron Transport, Models, Molecular, Oxidation-Reduction, Phylogeny, Protein Domains, Protein Multimerization, Zinc Fingers.

Abstract

Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides, used in DNA synthesis and repair. Two different mechanisms help deliver the required electrons to the RNR active site. Formate can be used as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cysteine pair, which then delivers the electrons to the active site. Here, we characterized a novel cysteine-rich C-terminal domain (CRD), which is present in most class II RNRs found in microbes. The NrdJd-type RNR from the bacterium Stackebrandtia nassauensis was used as a model enzyme. We show that the CRD is involved in both higher oligomeric state formation and electron transfer to the active site. The CRD-dependent formation of high oligomers, such as tetramers and hexamers, was induced by addition of dATP or dGTP, but not of dTTP or dCTP. The electron transfer was mediated by an array of six cysteine residues at the very C-terminal end, which also coordinated a zinc atom. The electron transfer can also occur between subunits, depending on the enzyme's oligomeric state. An investigation of the native reductant of the system revealed no interaction with glutaredoxins or thioredoxins, indicating that this class II RNR uses a different electron source. Our results indicate that the CRD has a crucial role in catalytic turnover and a potentially new terminal reduction mechanism and suggest that the CRD is important for the activities of many class II RNRs.

DOI: 10.1074/jbc.M117.806331
PubMed: 28972190
PubMed Central: PMC5704485

Affiliations:

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

to stream Main, to step Corpus: 000307
to stream Main, to step Curation: 000307

Le document en format XML

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<term>Actinomycetales (genetics)</term>
<term>Actinomycetales (metabolism)</term>
<term>Allosteric Regulation (MeSH)</term>
<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (genetics)</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Cysteine (chemistry)</term>
<term>Cysteine (genetics)</term>
<term>Cysteine (metabolism)</term>
<term>Electron Transport (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Phylogeny (MeSH)</term>
<term>Protein Domains (MeSH)</term>
<term>Protein Multimerization (MeSH)</term>
<term>Ribonucleotide Reductases (chemistry)</term>
<term>Ribonucleotide Reductases (genetics)</term>
<term>Ribonucleotide Reductases (metabolism)</term>
<term>Zinc Fingers (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Actinomycetales (composition chimique)</term>
<term>Actinomycetales (génétique)</term>
<term>Actinomycetales (métabolisme)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Cystéine (composition chimique)</term>
<term>Cystéine (génétique)</term>
<term>Cystéine (métabolisme)</term>
<term>Doigts de zinc (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Domaines protéiques (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Multimérisation de protéines (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Phylogenèse (MeSH)</term>
<term>Protéines bactériennes (composition chimique)</term>
<term>Protéines bactériennes (génétique)</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Ribonucleotide reductases (composition chimique)</term>
<term>Ribonucleotide reductases (génétique)</term>
<term>Ribonucleotide reductases (métabolisme)</term>
<term>Régulation allostérique (MeSH)</term>
<term>Transport d'électrons (MeSH)</term>
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<term>Cysteine</term>
<term>Ribonucleotide Reductases</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Actinomycetales</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Actinomycetales</term>
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<term>Protéines bactériennes</term>
<term>Ribonucleotide reductases</term>
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<term>Bacterial Proteins</term>
<term>Cysteine</term>
<term>Ribonucleotide Reductases</term>
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<term>Cystéine</term>
<term>Protéines bactériennes</term>
<term>Ribonucleotide reductases</term>
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<term>Bacterial Proteins</term>
<term>Cysteine</term>
<term>Ribonucleotide Reductases</term>
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<term>Protéines bactériennes</term>
<term>Ribonucleotide reductases</term>
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<term>Phylogeny</term>
<term>Protein Domains</term>
<term>Protein Multimerization</term>
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<term>Domaines protéiques</term>
<term>Modèles moléculaires</term>
<term>Multimérisation de protéines</term>
<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides, used in DNA synthesis and repair. Two different mechanisms help deliver the required electrons to the RNR active site. Formate can be used as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cysteine pair, which then delivers the electrons to the active site. Here, we characterized a novel cysteine-rich C-terminal domain (CRD), which is present in most class II RNRs found in microbes. The NrdJd-type RNR from the bacterium <i>Stackebrandtia nassauensis</i>
 was used as a model enzyme. We show that the CRD is involved in both higher oligomeric state formation and electron transfer to the active site. The CRD-dependent formation of high oligomers, such as tetramers and hexamers, was induced by addition of dATP or dGTP, but not of dTTP or dCTP. The electron transfer was mediated by an array of six cysteine residues at the very C-terminal end, which also coordinated a zinc atom. The electron transfer can also occur between subunits, depending on the enzyme's oligomeric state. An investigation of the native reductant of the system revealed no interaction with glutaredoxins or thioredoxins, indicating that this class II RNR uses a different electron source. Our results indicate that the CRD has a crucial role in catalytic turnover and a potentially new terminal reduction mechanism and suggest that the CRD is important for the activities of many class II RNRs.</div>
</front>
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<DateCompleted><Year>2018</Year>
<Month>10</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<Issue>46</Issue>
<PubDate><Year>2017</Year>
<Month>11</Month>
<Day>17</Day>
</PubDate>
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<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.</ArticleTitle>
<Pagination><MedlinePgn>19044-19054</MedlinePgn>
</Pagination>
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<Abstract><AbstractText>Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides, used in DNA synthesis and repair. Two different mechanisms help deliver the required electrons to the RNR active site. Formate can be used as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cysteine pair, which then delivers the electrons to the active site. Here, we characterized a novel cysteine-rich C-terminal domain (CRD), which is present in most class II RNRs found in microbes. The NrdJd-type RNR from the bacterium <i>Stackebrandtia nassauensis</i>
 was used as a model enzyme. We show that the CRD is involved in both higher oligomeric state formation and electron transfer to the active site. The CRD-dependent formation of high oligomers, such as tetramers and hexamers, was induced by addition of dATP or dGTP, but not of dTTP or dCTP. The electron transfer was mediated by an array of six cysteine residues at the very C-terminal end, which also coordinated a zinc atom. The electron transfer can also occur between subunits, depending on the enzyme's oligomeric state. An investigation of the native reductant of the system revealed no interaction with glutaredoxins or thioredoxins, indicating that this class II RNR uses a different electron source. Our results indicate that the CRD has a crucial role in catalytic turnover and a potentially new terminal reduction mechanism and suggest that the CRD is important for the activities of many class II RNRs.</AbstractText>
<CopyrightInformation>© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Loderer</LastName>
<ForeName>Christoph</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>From the Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jonna</LastName>
<ForeName>Venkateswara Rao</ForeName>
<Initials>VR</Initials>
<AffiliationInfo><Affiliation>the Department of Medical Biochemistry, Umeå University, SE-901 87 Umeå, Sweden.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Crona</LastName>
<ForeName>Mikael</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>From the Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden and.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Rozman Grinberg</LastName>
<ForeName>Inna</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>From the Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sahlin</LastName>
<ForeName>Margareta</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>From the Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hofer</LastName>
<ForeName>Anders</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>the Department of Medical Biochemistry, Umeå University, SE-901 87 Umeå, Sweden.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Lundin</LastName>
<ForeName>Daniel</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>From the Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden and daniel.lundin@dbb.su.se.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sjöberg</LastName>
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A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.

A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.

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