CE11 - Caractérisation des structures et relations structure-fonction des macro-molécules biologiques

A good grasp on the synthesis and role of glutaminylation post-translational modification – Q-TEF1

Submission summary

Post-translational modifications provide proteins with an extended repertoire to modulate their stability and function. A new modification of the eEF1A translation elongation factor: glutaminylation of a single glutamate, was reported recently. The synthesis, function and distribution of this original modification remain to be deciphered. Our previous work led us to serendipitously identify a protein required for the synthesis of this modification. Using enzymatic assays, in vivo analyses, proteomic data and structure determination we will investigate how this protein mediates eEF1A modification and the role of its different domains in this process. We will also explore the distribution of this modification in proteomes and identify the molecular function conferred by this modification. Structural analyses will complete these studies to provide a mechanistic understanding of protein glutaminylation and its consequences.

Project coordination

Bertrand SERAPHIN (Institut de Génétique et de Biologie Moléculaire et Cellulaire)

The author of this summary is the project coordinator, who is responsible for the content of this summary. The ANR declines any responsibility as for its contents.

Partner

BIOC Ecole Polytechnique
IGBMC Institut de Génétique et de Biologie Moléculaire et Cellulaire

Help of the ANR 409,587 euros
Beginning and duration of the scientific project: September 2022 - 48 Months

Useful links

Explorez notre base de projets financés

 

 

ANR makes available its datasets on funded projects, click here to find more.

Sign up for the latest news:
Subscribe to our newsletter