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The I2BC is a very large joint research unit of the CNRS, CEA, and Université Paris Saclay, located at Gif, Orsay, and Saclay sites. This doctoral position is available in the “Structures and Functions of Hybrid Assembly Chains of Natural Products” team within the Department of Microbiology, consisting of one CR-level researcher.
The project aims to determine the molecular mechanism of pyrimidine ring assembly during biosynthesis of the glycopeptide antibiotic/anticancer drug bleomycin by a
Organisation/Company CNRS Department Institut de Biologie Intégrative de la Cellule Research Field Chemistry Physics » Biophysics Biological sciences » Biological engineering Researcher Profile First Stage Researcher (R1) Application Deadline 20 Oct 2026 - 23:59 (UTC) Country France Type of Contract Temporary Job Status Full-time Hours Per Week 35 Offer Starting Date 1 Dec 2026 Is the job funded through the EU Research Framework Programme? Not funded by a EU programme Is the Job related to staff position within a Research Infrastructure? No
The I2BC is a very large joint research unit of the CNRS, CEA, and Université Paris Saclay, established on January 1, 2015. Located at the Gif, Orsay, and Saclay sites, the unit has an average staff of approximately 650 people distributed across 5 scientific departments, 43 research teams, and 17 high-level technology platforms.
The doctoral position is available in the “Structures and Functions of Hybrid Assembly Chains of Natural Products” team, which is part of the Department of Microbiology and consists of one CR-level researcher.
Drug resistance and toxicity highlight the urgent need for new strategies to discover and engineer bioactive natural products. This project aims to determine the molecular mechanism of pyrimidine ring assembly during the biosynthesis of the glycopeptide antibiotic/anticancer drug bleomycin by a nonribosomal peptide synthetase (NRPS) assembly line. Pyrimidine moieties are essential for the activities of numerous drugs, while the modular architecture of NRPSs makes them attractive platforms for bioengineering. Our project will combine biochemistry, structural biology, and chemical synthesis to define the catalytic mechanisms, structures, and protein-protein interactions responsible for NRPS-mediated pyrimidine formation. By elucidating how specialized NRPS domains cooperate to construct complex heterocycles, we will reveal the molecular basis of their unusual chemistry and the interaction interfaces that govern biosynthetic efficiency. These findings will establish a framework for rational NRPS engineering to produce novel pyrimidine-containing natural products with improved bioactivities, advancing sustainable approaches to combat drug resistance and toxicity.
Research Field Biological sciences » Biological engineering Years of Research Experience None