[Expired] 2 Years post-doctoral position available in Grenoble, ANR MASTIC project
Place of work: IRIG institute, CEA-Grenoble, Rhône-Alpes, France
Salary: ~2200 € / month
The Laboratory of Chemistry and Biology of Metals (LCBM) is a mixed laboratory (CEA, CNRS, Grenoble Alps University) that takes part of the IRIG institute at the CEA of Grenoble. The laboratory, at the interface between chemistry and biology, focuses on the study of the structure, activity and regulation of complex biological systems using or transporting metals.
A 2 years post-doctoral position is available at the LCBM in the “Biocatalysis” team (headed by S. Ollagnier de Choudens) which investigates the assembly and reactivity of iron-sulfur proteins at molecular level. The project is financed by the “Agence Nationale de la Recherche” (ANR).
Summary of the ANR MASTIC project:
Iron-sulfur (Fe-S) clusters are ancient and ubiquitous protein cofactors essential for life. Fe-S proteins contribute to multiple processes in bioenergetics, metabolism, gene expression, DNA transactions, and biosynthetic pathways. In both eukaryotes and prokaryotes, Fe-S cluster-containing proteins are initially synthesized as apo-proteins and the Fe-S cofactors are subsequently incorporated in a controlled way thanks to specific and complex multiprotein assembly machineries. In addition to the NIF machinery present in nitrogen-fixing bacteria and dedicated to the maturation of nitrogenase, bacteria express the ISC (Iron Sulfur Cluster) and/or SUF (SUlfur mobilization Factor) machineries that are present in eukaryote mitochondria and chloroplasts respectively. Eukaryotes also display a Cytosolic Iron-sulfur protein Assembly (CIA) machinery for the maturation of cytosolic and nuclear Fe-S proteins. In all these machineries, the de novo Fe-S cluster assembly process can be divided in two major steps. Firstly, Fe-S clusters are built on so-called scaffold proteins/complexes from iron and sulfur atoms delivered by dedicated proteins. The second step consists in the transfer of these preformed Fe-S clusters to recipient apo-proteins either directly or via dedicated Fe-S cluster transfer proteins. Based on the organization of the SUF operon in Escherichia coli, the SUF system was initially described as a machinery composed of six proteins (SufABCDSE), although the situation is in fact more complex, since additional factors are required. While the role of each of these proteins is rather clear, i.e. sulfur atoms are provided by the SUFS/SUFE couple, SUFBC2D is the scaffold complex which assembles and delivers its Fe-S cluster to the so-called A-type carrier (ATC) protein, SUFA, some unresolved questions remain about the role of the other players involved and about the molecular and structural details supporting specificity and dynamics of complex formation in both the assembly and transfer steps. The MASTIC project aims at addressing several key unsolved questions:
– How are iron atoms and electrons supplied to the SUF assembly complex?
– What type of Fe-S cluster is synthesized de novo on the SUFBC2D scaffold complex?
– What are the molecular mechanisms and structural dynamics in the assembly and transfer steps ?
The goal of the BioCat team in Grenoble, one of the team involved in the MASTIC project, is to characterize biochemically and spectroscopically the SUF components to understand how this Fe-S cluster biogenesis system works at a molecular level to assemble Fe-S clusters.
The candidates should have a strong expertise in biochemistry and an interest for spectroscopy and structural biology. Candidates should preferably have a 2 to 4 years research experience.