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Comment
. 2015 May 21;11(5):e1005192.
doi: 10.1371/journal.pgen.1005192. eCollection 2015 May.

Trading Places-Switching Frataxin Function by a Single Amino Acid Substitution within the [Fe-S] Cluster Assembly Scaffold

Dennis R Dean  1 , Patricia C Dos Santos  2
Affiliations
Comment

Trading Places-Switching Frataxin Function by a Single Amino Acid Substitution within the [Fe-S] Cluster Assembly Scaffold

Dennis R Dean et al. PLoS Genet. .
No abstract available

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Fig 1
Fig 1. Frataxin involvement in [Fe-S] cluster biogenesis in E. coli and S. cerevisiae.
Cysteine desulfurases IscS and Nfd1/Isd11 are shown in yellow, and the frataxin orthologs CyaY and Yfh1 are shown in red. The wild-type scaffold proteins IscU Ile108 and Isu1 Met141 are indicated in blue, while the variant proteins are in orange (IscU Met108 and Isu1 Ile141). In E. coli, CyaY has been shown to inhibit in vitro assembly of Fe-S cluster on wild-type IscU (indicated by red bar), and is required for in vivo [Fe-S] cluster biogenesis in strains containing IscU Met108 (indicated by black bar). In S. cerevisiae, Yfh1 facilitates [Fe-S] cluster assembly on the wild-type Isu1 (indicated by black bar), while a strain containing Isu1 Ile141 does not require Yfh1 for in vivo [Fe-S] cluster biogenesis.
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