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Getting further into NFU2 function in Fe-S clusters transfer, comparative proteome

ABSTRACT: A global quantitative label free (QLF) proteomic strategy was carried out comparing both the shoot and root proteomes of wild-type and nfu2 plants.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Root, Leaf

SUBMITTER: Nathalie Berger

LAB HEAD: Christian Dubos

PROVIDER: PXD015624 | Pride | 2020-07-06

REPOSITORIES: Pride

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			Action	DRS
	COL-1A_roots_proteome.raw	Raw
	COL-1B_roots_proteome.raw	Raw
	COL-1C_roots_proteome.raw	Raw
	COL-1D_roots_proteome.raw	Raw
	COL-2A_roots_proteome.raw	Raw

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Publications

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

Berger Nathalie N Vignols Florence F Przybyla-Toscano Jonathan J Roland Mélanie M Rofidal Valérie V Touraine Brigitte B Zienkiewicz Krzysztof K Couturier Jérémy J Feussner Ivo I Santoni Véronique V Rouhier Nicolas N Gaymard Frédéric F Dubos Christian C

Journal of experimental botany 20200701 14

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 protei ...[more]

PMID: 32240305

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