[en] About 50 proteins expressed in plastids of photosynthetic eukaryotes ligate iron‑sulfur (Fe-S) clusters and ensure vital functions in photosynthesis, sulfur and nitrogen assimilation, but also in the synthesis of pigments, vitamins and hormones. The synthesis of these Fe-S clusters, which are co- or post-translationally incorporated into these proteins, relies on several proteins belonging to the so-called sulfur mobilization (SUF) machinery. An Fe-S cluster is first de novo synthesized on a scaffold protein complex before additional late-acting maturation factors act in the specific transfer, possible conversion and insertion of this cluster into target recipient proteins. In this review, we will summarize what is known about the molecular mechanisms responsible for both the synthesis and transfer steps, focusing in particular on the structural aspects that allow the formation of the required protein complexes.
F.R.S.-FNRS - Fonds de la Recherche Scientifique ANR - Agence Nationale de la Recherche
Funding text :
The UMR1136 is supported by a grant overseen by the French National
Research Agency (ANR) as part of the “Investissements d’Avenir”
program (ANR-11-LABX-0002-01, Lab of Excellence ARBRE). The work
about the chloroplastic SUF machinery is supported by a grant awarded
by the French National Research Agency (ANR-22-CE20-0039-01) to N.
R. A. K. is recipient of a research fellow from Fonds de la Recherche
Scientifique — FNRS (F.R.S.-FNRS). C.R. acknowledges F.R.S.-FNRS
(CDR J.0149.23).
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