An I2BC team has revealed the structure of the C-terminal transmembrane region of the SARS-CoV-2 protein nsp3, essential for virus replication. This region self-assembles into hexamers that form molecular pores on the surface of double-membrane vesicles, the sites of viral genome replication. Nsp3 therefore appears to be a promising therapeutic target.

A team from I2BC has studied the positioning of nucleosomes in the yeast S cerevisiae genome, using an original mathematical method to analyze next-generation sequencing data. This mapping highlights the role of chromatin remodeling complexes in nucleosome organization.

Teams from I2BC, Institut Curie and IRB shed light on how the human nuclease MRN works. Structural predictions obtained with AlphaFold2 and confirmed by in vitro and in vivo experiments show that the phosphorylated Sae2/CtIP protein forms a network of interactions with MRN that favours the removal of its autoinhibition.

Using a range of spectroscopic techniques, researchers at I2BC in collaboration with ICMMO have elucidated the catalytic cycle of a bio-inspired iron porphyrin catalyst, which could form the basis of economically viable solutions for the conversion and recovery of CO2.

Researchers from the AMIG team (I2BC department), in collaboration with the IRB (Switzerland), have modeled the interaction between HROB and the helicases MCM8-MCM9, some mutations of which predispose individuals to infertility or cancer. They demonstrate that HROB promotes the catalytic activity of the MCM8-MCM9 complex but does not play a role in its recruitment or stability.