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

• Published in: Scientific reports Vol. 9; no. 1; p. 712
• Main Authors: Pardoux, Romain, Fiévet, Anouchka, Carreira, Cíntia, Brochier-Armanet, Céline, Valette, Odile, Dermoun, Zorah, Py, Béatrice, Dolla, Alain, Pauleta, Sofia R., Aubert, Corinne
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 24.01.2019; Nature Publishing Group
• Subjects: 101/28; 14/35; 14/63; 38; 38/77; 45; 45/29; 631/326/41/2095; 631/45/612/1141; 82/80; 82/83; Aerobic bacteria; ATP; ATP-binding protein; Biosynthesis; Fluorescence microscopy; Humanities and Social Sciences; Hydrolase; Iron; Iron-sulfur proteins; Kinases; Life Sciences; Localization; Molybdenum; multidisciplinary; Proteins; Science; Science (multidisciplinary); Sulfur; Metalloproteins; Bacterial systems biology
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-018-37021-8

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.