Abstract
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.
Highlights
To perform an accurate protein synthesis, ribosomes accomplish complex tasks involving the longrange communication between its functional centres such as the peptidyl transfer centre, the tRNA bindings sites and the peptide exit tunnel
Comparing the three kingdoms’ networks makes it possible to identify the evolutionary status of all their components (Supplementary Tables 1 and 2) and to trace how they have developed over time
The Bacterial (B), Archaeal (A) and Eukaryotic (E) networks have gradually developed through the addition of new proteins and/or new connections
Summary
To perform an accurate protein synthesis, ribosomes accomplish complex tasks involving the longrange communication between its functional centres such as the peptidyl transfer centre, the tRNA bindings sites and the peptide exit tunnel. While the past decade studies have provided a detailed mechanistic understanding of almost all of the translation steps, one of the major challenges in ribosome research is how information is transmitted and processed between remote functional sites such as the tRNA binding sites, the peptidyl-transfer centre (PTC) and the peptide exit tunnel, during protein synthesis. Communication processes coordinate the complex ribosomal movements during translation, such as the ratchet-like motion between the two s ubunits[35,36,37] In addition to their roles in rRNA folding and ribosome a ssembly[38,39,40,41,42,43], extensions systematically form complex r-protein networks through tiny interactions, in the three kingdom ribosomes[2,3,44]. Several questions remain to be answered: are the tiny interfaces structurally and phylogenetically conserved in the three domains of life? How has r-protein network connectivity evolved over time and does graph theory provide information about their evolution and functionality? Here, we present a global study of the evolution of r-protein networks, through a phylogenetic, structural and mathematical analysis of their architectures
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
