Post-transcriptional association of proteins to study spatial organisation within multi-enzyme complexes

Cédric Y Montanier (1) , Louise Badruna (1) , Vincent Burlat (2) , Pierre Roblin (3, 4) , Thomas Lautier (1) , Tiffany Chau (5) , Claire Dumon (1)

1 TBI - Toulouse Biotechnology Institute
2 Dynamique et Evolution des Parois cellulaires végétales
3 CEPIA - Département Caractérisation et Elaboration des Produits Issus de l'Agriculture
4 SSOLEIL - Synchrotron SOLEIL
5 SIFBI - Singapore Institute of Food and Biotechnology Innovation

To catalyse chemical reactions, nature has evolved enzymatic cascades. These multistep reactions in living cells are often performed by multi-enzyme complexes to maintain high local concentrations of intermediates to enhance reaction rates, called substrate channelling. Based on the fact that natural proteins or nucleic acid-protein interactions can be used as scaffolds for the construction of functional multi-enzyme complexes, artificial scaffolds have been developed for the construction of multi-enzyme complexes which carry out multi-step enzymatic catalysis processes1. However, none of them have systematically investigated the spatial organisation of the enzymes and its effect on the product(s) released. We are investigating this question using the Molecular Welding Tool2 consisting of two small proteins, Jo and In, which spontaneously form an intramolecular isopeptide bond and, incidentally, provide an original means of orienting enzymes3,4.

Domaines: Sciences de l'environnement; Sciences du Vivant [q-bio]

Cédric Y Montanier, Louise Badruna, Vincent Burlat, Pierre Roblin, Thomas Lautier, et al.. Post-transcriptional association of proteins to study spatial organisation within multi-enzyme complexes. Enzyme Engineering XXVII, Oct 2023, Singapoure, Singapore. ⟨hal-04225770⟩