4.5 Article

Conserved functions of Arabidopsis mitochondrial late-acting maturation factors in the trafficking of iron-sulfur clusters

期刊

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2018.06.003

关键词

Iron-sulfur cluster; Late-acting maturation factors; ISC machinery; Arabidopsis; Yeast complementation

资金

  1. Agence Nationale de la Recherche [ANR-2013-BSV6-0002-01]
  2. French National Research Agency (ANR) as part of the Investissements d'Avenir program (Lab of Excellence ARBRE) [ANR-11-LABX-0002-01]
  3. Deutsche Forschungsgemeinschaft [SFB987, SPP 1710, 1927]
  4. LOEWE program of state Hessen

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Numerous proteins require iron-sulfur (Fe-S) clusters as cofactors for their function. Their biogenesis is a multi-step process occurring in the cytosol and mitochondria of all eukaryotes and additionally in plastids of photosynthetic eukaryotes. A basic model of Fe-S protein maturation in mitochondria has been obtained based on studies achieved in mammals and yeast, yet some molecular details, especially of the late steps, still require investigation. In particular, the late-acting biogenesis factors in plant mitochondria are poorly understood. In this study, we expressed the factors belonging to NFU, BOLA, SUFA/ISCA and IBA57 families in the respective yeast mutant strains. Expression of the Arabidopsis mitochondrial orthologs was usually sufficient to rescue the growth defects observed on specific media and/or to restore the abundance or activity of the defective Fe-S or lipoic acid-dependent enzymes. These data demonstrate that the plant mitochondrial counterparts, including duplicated isoforms, likely retained their ancestral functions. In contrast, the SUFA1 and IBA57.2 plastidial isoforms cannot rescue the lysine and glutamate auxotrophies of the respective isal-isa24 and iba574 strains or of the isal-isa2-iba57A triple mutant when expressed in combination. This suggests a specialization of the yeast mitochondrial and plant plastidial factors in these late steps of Fe-S protein biogenesis, possibly reflecting substrate-specific interactions in these different compartments.

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