F. Rao
Co-evolution of quaternary organization and novel RNA tertiary interactions revealed in the crystal structure of a bacterial protein–RNA toxin–antitoxin system
Rao, F.; Short, F.L.; Voss, J.E.; Blower, T.R.; Orme, A.L.; Whittaker, T.E.; Luisi, B.F.; Salmond, G.P.C.
Authors
F.L. Short
J.E. Voss
Professor Tim Blower timothy.blower@durham.ac.uk
Professor
A.L. Orme
T.E. Whittaker
B.F. Luisi
G.P.C. Salmond
Abstract
Genes encoding toxin–antitoxin (TA) systems are near ubiquitous in bacterial genomes and they play key roles in important aspects of bacterial physiology, including genomic stability, formation of persister cells under antibiotic stress, and resistance to phage infection. The CptIN locus from Eubacterium rectale is a member of the recently-discovered Type III class of TA systems, defined by a protein toxin suppressed by direct interaction with a structured RNA antitoxin. Here, we present the crystal structure of the CptIN protein–RNA complex to 2.2 Å resolution. The structure reveals a new heterotetrameric quaternary organization for the Type III TA class, and the RNA antitoxin bears a novel structural feature of an extended A-twist motif within the pseudoknot fold. The retention of a conserved ribonuclease active site as well as traits normally associated with TA systems, such as plasmid maintenance, implicates a wider functional role for Type III TA systems. We present evidence for the co-variation of the Type III component pair, highlighting a distinctive evolutionary process in which an enzyme and its substrate co-evolve.
Citation
Rao, F., Short, F., Voss, J., Blower, T., Orme, A., Whittaker, T., …Salmond, G. (2015). Co-evolution of quaternary organization and novel RNA tertiary interactions revealed in the crystal structure of a bacterial protein–RNA toxin–antitoxin system. Nucleic Acids Research, 43(19), 9529-9540. https://doi.org/10.1093/nar/gkv868
Journal Article Type | Article |
---|---|
Acceptance Date | Aug 17, 2015 |
Online Publication Date | Sep 8, 2015 |
Publication Date | Oct 30, 2015 |
Deposit Date | Sep 28, 2015 |
Publicly Available Date | Oct 5, 2015 |
Journal | Nucleic Acids Research |
Print ISSN | 0305-1048 |
Electronic ISSN | 1362-4962 |
Publisher | Oxford University Press |
Peer Reviewed | Peer Reviewed |
Volume | 43 |
Issue | 19 |
Pages | 9529-9540 |
DOI | https://doi.org/10.1093/nar/gkv868 |
Files
Published Journal Article (Advance online version)
(13.3 Mb)
PDF
Publisher Licence URL
http://creativecommons.org/licenses/by/4.0/
Copyright Statement
Advance online version © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
Published Journal Article (Final published version)
(608 Kb)
PDF
Publisher Licence URL
http://creativecommons.org/licenses/by/4.0/
Copyright Statement
Final published version
You might also like
Viruses wrap up bacterial defence systems
(2023)
Journal Article
Diverse Durham collection phages demonstrate complex BREX defence responses
(2023)
Journal Article
Downloadable Citations
About Durham Research Online (DRO)
Administrator e-mail: dro.admin@durham.ac.uk
This application uses the following open-source libraries:
SheetJS Community Edition
Apache License Version 2.0 (http://www.apache.org/licenses/)
PDF.js
Apache License Version 2.0 (http://www.apache.org/licenses/)
Font Awesome
SIL OFL 1.1 (http://scripts.sil.org/OFL)
MIT License (http://opensource.org/licenses/mit-license.html)
CC BY 3.0 ( http://creativecommons.org/licenses/by/3.0/)
Powered by Worktribe © 2024
Advanced Search