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

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 MrpORP associating a P-loop NTPase domain with a dinitrogenase iron-molybdenum cofactor biosynthesis domain (Di-Nase). Characterization of full length MrpORP, 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 MrpORP 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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The French National Research Agency (ANR) funded this research project (ANR-12-ISV8-0003-01). This work was supported by Fundacao para a Ciencia e Tecnologia (FCT) (grant to SRP, FCT-ANR/BBB-MET/0023/2012, and to CC, SFRH/BD/87898/2012) and by the Belgian Federal Science Policy Office (Belspo) (grant to BD, IAP7/44, iPROS project). Unidade de Ciencias Biomoleculares Aplicadas-UCIBIO was financed by national funds from FCT/MEC (UID/Multi/04378/2013) and co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728). This article is based upon work from COST Action CA15133, supported by COST (European Cooperation in Science and Technology).