The "Emergence program" promoted by the "Ville de Paris" is awarded to projects encouraging the creation and the development of new research teams in the Paris region.
Zhou Xu received one of these recognitions for 2019.
 

Nonribosomal peptide synthetases (NRPSs) are microbial megaenzymes that make a wide variety of small-molecule products, including many that are clinically used as antitumors, antibiotics, or immunosuppressants. Peptide synthesis proceeds with assembly-line logic, where each station on the NRPS assembly line is a multidomain unit called a module. While the function of single modules is well studied, much less is known how they work together. Researchers from the Schmeing lab at McGill University have resolved several dimodular NRPS structures, which show coordinated interactions between modules, and large conformational changes between catalytically relevant states. Martin Weigt from the “Statstical Genomics and Biological Physics” team has performed complementary coevolutionary analyses using the direct coupling analysis (DCA), which confirm the biological relevance and evolutionary conservation of the observed inter-modular interactions. DCA analysis has also allowed to suggest mutations in a module-swapped chimeric NRPS protein, which significantly increased the activity of the protein, a result of direct relevance toward the longstanding goal of NRPS bioengineering for production of new-to-nature bioactive small molecules.

Link to article in Science

GEMME makes the cover of the MBE november issue.

GEMME is a fast, scalable and simple method to predict mutational landscapes from natural sequences. It demonstrates how deleterious effects of a protein mutation are identified by looking at the closest known sequence accepting the mutation in the evolutionary tree of sequences and at its epistatic changes.  The article just appeared in Molecular Biology and Evolution.

Link to the article
Link to the webserver 
 

We propose the concept of "interacting region" and the dynJET2 method toward deciphering the complexity underlying protein surface usage and deformability. Interacting regions account for the multiple usage of a protein's surface residues by several partners and for the variability of protein interfaces coming from molecular flexibility. dynJET2 predicts interacting patches by crossing evolutionary, physico‐chemical and geometrical properties of the protein surface with information coming from complete cross‐docking (CC‐D) simulations. 

Link to the Article

The Team of Diatom Functional Genomics (R. Annunziata, A. Ritter, A.E. Fortunato, A. Manzotti, S. Cheminant Navarro, J.P. Bouly and A. Falciatore), in collaboration with the team of Biology of Genomes (Nicolas Agier) and Marco Cosentino Lagomarsino at the LCQB characterized the circadian rhythms of the marine diatom Phaeodactylum tricornutum and identified the bHLH-PAS protein RITMO1 as the first known regulator of these rhythms in these algae. This study, published on Proceedings of the National Academy of Sciences (PNAS) adds new elements to our understanding of diatom biology and offers new perspectives to elucidate timekeeping mechanisms in marine algae.