Identification of client iron-sulfur proteins of the chloroplastic NFU2 transfer protein in Arabidopsis thaliana
2020
Berger, Nathalie | Vignols, Florence | Przybyla-Toscano, Jonathan | Roland, Mélanie | Rofidal, Valerie | Touraine, Brigitte | Zienkiewicz, Krzysztof | Couturier, Jérémy | Feussner, Ivo | Santoni, Veronique | Rouhier, Nicolas | Gaymard, Frédéric | Dubos, Christian | Biochimie et Physiologie Moléculaire des Plantes (BPMP) ; Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Interactions Arbres-Microorganismes (IAM) ; Université de Lorraine (UL)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Plateforme de Spectrométrie de Masse Protéomique - Mass Spectrometry Proteomics Platform (MSPP) ; Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Albrecht von Haller Institute for Plant Sciences Department of Plant Biochemistry ; Georg-August-University of Göttingen = Georg-August-Universität Göttingen | Georg-August-University of Göttingen = Georg-August-Universität Göttingen | ANR-11-LABX-0002,ARBRE,Recherches Avancées sur l'Arbre et les Ecosytèmes Forestiers(2011) | ANR-15-IDEX-0004,LUE,Isite LUE(2015)
International audience
Show more [+] Less [-]English. Iron-sulfur (Fe-S) proteins have critical functions in plastids, participating notably in the photosynthetic electron transfer, sulfur and nitrogen assimilation, chlorophyll metabolism and vitamin or amino acid biosynthesis. Their maturation relies on the so-called SUF assembly machinery. The 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 towards 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 have performed a quantitative proteomic analysis of nfu2 plants (shoots, roots and seedlings). 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 (BiFC) assay. These analyses also revealed a possible role for NFU2 in plant response to desiccation. Altogether this study delineates better the maturation pathways of many chloroplastic Fe-S proteins, extending considerably the number of NFU2 clients. It also helps clarifying the respective roles of the three NFU paralogs, NFU1, NFU2 and NFU3.
Show more [+] Less [-]AGROVOC Keywords
Bibliographic information
This bibliographic record has been provided by Institut national de la recherche agronomique