The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis - Aix-Marseille Université Access content directly
Journal Articles Scientific Reports Year : 2019

The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis

Abstract

Despite recent advances in understanding the biogenesis of iron-sulfur (Fe-S) proteins, most studies focused on aerobic bacteria as model organisms. Accordingly, multiple players have been proposed to participate in the Fe-S delivery step to apo-target proteins, but critical gaps exist in the knowledge of Fe-S proteins biogenesis in anaerobic organisms. Mrp/NBP35 ATP-binding proteins are a subclass of the soluble P-loop containing nucleoside triphosphate hydrolase superfamily (P-loop NTPase) known to bind and transfer Fe-S clusters in vitro. Here, we report investigations of a novel atypical two-domain Mrp/NBP35 ATP-binding protein named Mrp ORP associating a P-loop NTPase domain with a dinitrogenase iron-molybdenum cofactor biosynthesis domain (Di-Nase). Characterization of full length Mrp ORP , as well as of its two domains, showed that both domains bind Fe-S clusters. We provide in vitro evidence that the P-loop NTPase domain of the Mrp ORP can efficiently transfer its Fe-S cluster to apo-target proteins of the ORange Protein (ORP) complex, suggesting that this novel protein is involved in the maturation of these Fe-S proteins. Last, we showed for the first time, by fluorescence microscopy imaging a polar localization of a Mrp/NBP35 protein.
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hal-02186929 , version 1 (17-07-2019)

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Romain Pardoux, Anouchka Fiévet, Cíntia Carreira, Céline Brochier-Armanet, Odile Valette, et al.. The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis. Scientific Reports, 2019, 9 (1), pp.360-373. ⟨10.1038/s41598-018-37021-8⟩. ⟨hal-02186929⟩
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