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Revising the structural diversity of ribosomal proteins across the three domains of life

Lookup NU author(s): Dr Sergey MelnikovORCiD



This is the authors' accepted manuscript of an article that has been published in its final definitive form by Oxford University Press, 2018.

For re-use rights please refer to the publisher's terms and conditions.


© The Author(s) 2018. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved.Ribosomal proteins are indispensable components of a living cell, and yet their structures are remarkably diverse in different species. Here we use manually curated structural alignments to provide a comprehensive catalog of structural variations in homologous ribosomal proteins from bacteria, archaea, eukaryotes, and eukaryotic organelles. By resolving numerous ambiguities and errors of automated structural and sequence alignments, we uncover a whole new class of structural variations that reside within seemingly conserved segments of ribosomal proteins.We then illustrate that these variations reflect an apparent adaptation of ribosomal proteins to the specific environments and lifestyles of living species. Finally, we show that most of these structural variations reside within nonglobular extensions of ribosomal proteins-protein segments that are thought to promote ribosome biogenesis by stabilizing the proper folding of ribosomal RNA.We show that although the extensions are thought to be themost ancient peptides on our planet, they are in fact themost rapidly evolving andmost structurally and functionally diverse segments of ribosomal proteins. Overall, our work illustrates that, despite being long considered as slowly evolving and highly conserved, ribosomal proteins are more complex and more specialized than is generally recognized.

Publication metadata

Author(s): Melnikov S, Manakongtreecheep K, Soll D

Publication type: Article

Publication status: Published

Journal: Molecular Biology and Evolution

Year: 2018

Volume: 35

Issue: 7

Pages: 1588-1598

Print publication date: 01/07/2018

Online publication date: 24/02/2018

Acceptance date: 02/04/2016

Date deposited: 16/07/2020

ISSN (print): 0737-4038

ISSN (electronic): 1537-1719

Publisher: Oxford University Press


DOI: 10.1093/molbev/msy021

PubMed id: 29529322


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