Since 2009, Head of Laboratory of Physical and Chemical Biology of Membrane Proteins UMR7099 CNRS University Paris-Diderot, Paris, France.
The laboratory is worldwide known for the atomic structure of the membrane photosynthetic complex b6f and for the development by Jean Luc Popot and co-workers of amphipathic polymers, named Amphipols, that keep membrane proteins in solution .
I have introduced two new subjects within the unit:
1. The mitochondrial uncoupling protein UCPs with the long term objective to address the fundamental question of how do they transport protons.
2. The second project is about bio-production of membrane proteins, a subject that I initiated in John Walker laboratory (Cambridge, UK see below). Our long term goal is to design a adapted bacterial host for large scale membrane proliferation and membrane protein production.
Group leader in Daniel Ricquier’s laboratory, Hopital Necker, Paris , France 1997-2009
Ricquier’s lab discovered the mitochondrial uncoupling 2 gene and was the first construct Ucp2 knock out mice . Later on, I have shown that UCP2 modulate reactive oxygen production and promote fatty acid oxidation. Human genetic studies and transgenic mice model pointed out UCP2 as a key gene in inflammation by promoting immune cells activation and proliferation [3-6].
Post-doctoral work: 1993-1997 in John E Walker laboratory (Nobel Prize Winner Chemistry, 1997), Cambridge, Laboratory of Molecular Biology, MRC
Using a simple bacterial genetics approache, I derived T7 RNA polymerase bacterial expression hosts, C41(DE3) and C43(DE3), that are adapted to the large scale production of soluble and membrane proteins (, cited over 1000 times Google Scholar). In these mutant hosts, some membrane proteins trigger internal membrane proliferation opening the way to in vivo structural investigation of membrane proteins . A large number of membrane proteins have been crystallized after overproduction in those bacterial strains.
PhD work: laboratory of Dr Daniel Ricquier (CEREMOD, Meudon, France) 1989-93
The Uncoupling Protein (UCP) from brown adipose tissue dissipates the mitochondrial proton electrochemical gradient. In order to understand the molecular basis of heat production by UCP, I have evidenced the first experimental topological model , a model confirmed ten years later by the first x-ray structure of the ADP/ATP exchangor .