Graille Lab

Graille Lab

@graillelab.bsky.social

The GrailleLab is interested in understanding how RNA post-transcriptional and/or protein post-translational modifications are written, erased and read as well as how they influence mRNA decoding by ribosome for protein synthesis.

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Carola Doerr
@caroladoerr.bsky.social

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TanentzapfLab
@tanentzapflab.bsky.social

1. I feel like this is such obvious advice that it gets taken for granted & consequently no one says this to young scientists but READ PAPERS, read all the papers. As you move up in your career you will have less & less time to do this. Read everything that appeals to you not just in your field

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Kasia Siudeja
@ksiudeja.bsky.social

📣📣📣 Come join us and set up your team in the I2BC Cell Bio Dept! You will find great science, diverse topics and models, spacious labs, supportive environment, and fun colleagues. We are a short (train) ride south of Paris. Please DM me with any questions and help us spread the word 🙏

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Graille Lab
@graillelab.bsky.social

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.

Graille Lab
@graillelab.bsky.social

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.

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Graille Lab
@graillelab.bsky.social

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.

Graille Lab
@graillelab.bsky.social

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.

Graille Lab
@graillelab.bsky.social

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.

Graille Lab
@graillelab.bsky.social

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.

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