Evolution of ribosomal protein network architectures release_bnvaedeadjddlctx7s6bakt7bu

by Youri Timsit, Grégoire Sergeant-Perthuis, Daniel Bennequin

Published in Scientific Reports by Springer Science and Business Media LLC.

2021   Volume 11, Issue 1, p625

Abstract

<jats:title>Abstract</jats:title>To perform an accurate protein synthesis, ribosomes accomplish complex tasks involving the long-range communication between its functional centres such as the peptidyl transfer centre, the tRNA bindings sites and the peptide exit tunnel. How information is transmitted between these sites remains one of the major challenges in current ribosome research. Many experimental studies have revealed that some r-proteins play essential roles in remote communication and the possible involvement of r-protein networks in these processes have been recently proposed. Our phylogenetic, structural and mathematical study reveals that of the three kingdom's r-protein networks converged towards non-random graphs where r-proteins collectively coevolved to optimize interconnection between functional centres. The massive acquisition of conserved aromatic residues at the interfaces and along the extensions of the newly connected eukaryotic r-proteins also highlights that a strong selective pressure acts on their sequences probably for the formation of new allosteric pathways in the network.
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