Pas sûr qu'ils atteignent 25% des labos avec ces critères. Ils pourront faire encore plus d'économies. C'est Bercy qui va être content de ces bons élèves...

L´ingénieur viendra renforcer notre unité et en particulier mon équipe www.ferreiracercalab.com.

Merci de partager cette information.

Pour tous renseignements complémentaires, n´hésitez pas à nous solliciter.

Cool initiative. Could you please add my lab to this list? Thanks

This project was done in collaboration with the groups of Hervé LE HIR (IBENS, Paris) and Cosmin Saveanu (Institut Pasteur) with the support from ANR (Agence nationale de la recherche), CNRS, École Polytechnique and Fondation ARC pour la recherche sur le cancer.

Altogether, these results suggest that, during evolution, a general mechanism has been preserved to ensure the correct decay of aberrant mRNAs containing premature stop codons or transcripts with long 3’-UTRs.

This UPF1-SMG6 interaction turns out to be important for the optimal degradation of NMD substrates in human cells. These data demonstrate that the Upf1-Nmd4 interaction is conserved in human, reinforcing the existence of a universal mechanism for the NMD pathway.

We show that this region is important for the previously described phospho-independent interaction of the human SMG6 protein with the helicase domain of UPF1 and binds in a very similar way as yeast Nmd4 to UPF1 helicase domain.

We also show that Nmd4 activates the ATPase activity of Upf1 and increases its affinity for RNA. Interestingly, we identify a region similar to yeast Nmd4 C-terminal arm in metazoan SMG6, the main enzyme that initiates RNA degradation in metazoan NMD.

This article describes the crystal structure of the complex formed between the S. cerevisiae Nmd4 protein and the helicase domain of the Upf1 protein. This structure reveals that Nmd4 interacts with Upf1 helicase core through a conserved C-terminal arm.