Serveur d'exploration cluster fer-soufre

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Identification of client iron-sulfur proteins of the chloroplastic NFU2 transfer protein in Arabidopsis thaliana.

Identifieur interne : 000107 ( Main/Exploration ); précédent : 000106; suivant : 000108

Identification of client iron-sulfur proteins of the chloroplastic NFU2 transfer protein in Arabidopsis thaliana.

Auteurs : Nathalie Berger [France] ; Florence Vignols [France] ; Jonathan Przybyla-Toscano [France] ; Mélanie Roland [France] ; Valérie Rofidal [France] ; Brigitte Touraine [France] ; Krzysztof Zienkiewicz [Allemagne] ; Jérémy Couturier [France] ; Ivo Feussner [Allemagne] ; Véronique Santoni [France] ; Nicolas Rouhier [France] ; Frédéric Gaymard [France] ; Christian Dubos [France]

Source :

RBID : pubmed:32240305

Abstract

Iron-sulfur (Fe-S) proteins have critical functions in plastids, notably participating in photosynthetic electron transfer, sulfur and nitrogen assimilation, chlorophyll metabolism, and vitamin or amino acid biosynthesis. Their maturation relies on the so-called SUF (sulfur mobilization) assembly machinery. Fe-S clusters are synthesized de novo on a scaffold protein complex and then delivered to client proteins via several transfer proteins. However, the maturation pathways of most client proteins and their specificities for transfer proteins are mostly unknown. In order to decipher the proteins interacting with the Fe-S cluster transfer protein NFU2, one of the three plastidial representatives found in Arabidopsis thaliana, we performed a quantitative proteomic analysis of shoots, roots, and seedlings of nfu2 plants, combined with NFU2 co-immunoprecipitation and binary yeast two-hybrid experiments. We identified 14 new targets, among which nine were validated in planta using a binary bimolecular fluorescence complementation assay. These analyses also revealed a possible role for NFU2 in the plant response to desiccation. Altogether, this study better delineates the maturation pathways of many chloroplast Fe-S proteins, considerably extending the number of NFU2 clients. It also helps to clarify the respective roles of the three NFU paralogs NFU1, NFU2, and NFU3.

DOI: 10.1093/jxb/eraa166
PubMed: 32240305


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<div type="abstract" xml:lang="en">Iron-sulfur (Fe-S) proteins have critical functions in plastids, notably participating in photosynthetic electron transfer, sulfur and nitrogen assimilation, chlorophyll metabolism, and vitamin or amino acid biosynthesis. Their maturation relies on the so-called SUF (sulfur mobilization) assembly machinery. Fe-S clusters are synthesized de novo on a scaffold protein complex and then delivered to client proteins via several transfer proteins. However, the maturation pathways of most client proteins and their specificities for transfer proteins are mostly unknown. In order to decipher the proteins interacting with the Fe-S cluster transfer protein NFU2, one of the three plastidial representatives found in Arabidopsis thaliana, we performed a quantitative proteomic analysis of shoots, roots, and seedlings of nfu2 plants, combined with NFU2 co-immunoprecipitation and binary yeast two-hybrid experiments. We identified 14 new targets, among which nine were validated in planta using a binary bimolecular fluorescence complementation assay. These analyses also revealed a possible role for NFU2 in the plant response to desiccation. Altogether, this study better delineates the maturation pathways of many chloroplast Fe-S proteins, considerably extending the number of NFU2 clients. It also helps to clarify the respective roles of the three NFU paralogs NFU1, NFU2, and NFU3.</div>
</front>
</TEI>
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<MedlineCitation Status="In-Data-Review" Owner="NLM">
<PMID Version="1">32240305</PMID>
<DateRevised>
<Year>2020</Year>
<Month>07</Month>
<Day>07</Day>
</DateRevised>
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<Journal>
<ISSN IssnType="Electronic">1460-2431</ISSN>
<JournalIssue CitedMedium="Internet">
<Volume>71</Volume>
<Issue>14</Issue>
<PubDate>
<Year>2020</Year>
<Month>Jul</Month>
<Day>06</Day>
</PubDate>
</JournalIssue>
<Title>Journal of experimental botany</Title>
<ISOAbbreviation>J Exp Bot</ISOAbbreviation>
</Journal>
<ArticleTitle>Identification of client iron-sulfur proteins of the chloroplastic NFU2 transfer protein in Arabidopsis thaliana.</ArticleTitle>
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<MedlinePgn>4171-4187</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1093/jxb/eraa166</ELocationID>
<Abstract>
<AbstractText>Iron-sulfur (Fe-S) proteins have critical functions in plastids, notably participating in photosynthetic electron transfer, sulfur and nitrogen assimilation, chlorophyll metabolism, and vitamin or amino acid biosynthesis. Their maturation relies on the so-called SUF (sulfur mobilization) assembly machinery. Fe-S clusters are synthesized de novo on a scaffold protein complex and then delivered to client proteins via several transfer proteins. However, the maturation pathways of most client proteins and their specificities for transfer proteins are mostly unknown. In order to decipher the proteins interacting with the Fe-S cluster transfer protein NFU2, one of the three plastidial representatives found in Arabidopsis thaliana, we performed a quantitative proteomic analysis of shoots, roots, and seedlings of nfu2 plants, combined with NFU2 co-immunoprecipitation and binary yeast two-hybrid experiments. We identified 14 new targets, among which nine were validated in planta using a binary bimolecular fluorescence complementation assay. These analyses also revealed a possible role for NFU2 in the plant response to desiccation. Altogether, this study better delineates the maturation pathways of many chloroplast Fe-S proteins, considerably extending the number of NFU2 clients. It also helps to clarify the respective roles of the three NFU paralogs NFU1, NFU2, and NFU3.</AbstractText>
<CopyrightInformation>© The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissions@oup.com.</CopyrightInformation>
</Abstract>
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<Author ValidYN="Y">
<LastName>Berger</LastName>
<ForeName>Nathalie</ForeName>
<Initials>N</Initials>
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<Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
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<LastName>Vignols</LastName>
<ForeName>Florence</ForeName>
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<Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
</AffiliationInfo>
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<LastName>Przybyla-Toscano</LastName>
<ForeName>Jonathan</ForeName>
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<Affiliation>Université de Lorraine, INRAE, IAM, Nancy, France.</Affiliation>
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<ForeName>Mélanie</ForeName>
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<Affiliation>Université de Lorraine, INRAE, IAM, Nancy, France.</Affiliation>
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<ForeName>Valérie</ForeName>
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<Affiliation>Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences and Göttingen Center for Molecular Biosciences (GZMB), University of Göttingen, Göttingen, Germany.</Affiliation>
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<ForeName>Ivo</ForeName>
<Initials>I</Initials>
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<Affiliation>Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences and Göttingen Center for Molecular Biosciences (GZMB), University of Göttingen, Göttingen, Germany.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Service unit for Metabolomics and Lipidomics, Göttingen Center for Molecular Biosciences (GZMB), University of Göttingen, Göttingen, Germany.</Affiliation>
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<ForeName>Véronique</ForeName>
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</AffiliationInfo>
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<ForeName>Frédéric</ForeName>
<Initials>F</Initials>
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<Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
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<LastName>Dubos</LastName>
<ForeName>Christian</ForeName>
<Initials>C</Initials>
<AffiliationInfo>
<Affiliation>BPMP, Université de Montpellier, CNRS, INRAE, SupAgro, Montpellier, France.</Affiliation>
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<Country>England</Country>
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<ISSNLinking>0022-0957</ISSNLinking>
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<Keyword MajorTopicYN="N">Arabidopsis</Keyword>
<Keyword MajorTopicYN="N">NFU2</Keyword>
<Keyword MajorTopicYN="N">chloroplast</Keyword>
<Keyword MajorTopicYN="N">iron–sulfur cluster</Keyword>
<Keyword MajorTopicYN="N">protein–protein interactions</Keyword>
<Keyword MajorTopicYN="N">quantitative proteomic analysis</Keyword>
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