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An Atlas of the base inter-RNA stacks involved in bacterial translation.

Authors :
Ali Z
Kukhta T
Trant JF
Sharma P
Source :
Biophysical chemistry [Biophys Chem] 2024 Feb; Vol. 305, pp. 107144. Date of Electronic Publication: 2023 Dec 02.
Publication Year :
2024

Abstract

Nucleobase-specific noncovalent interactions play a crucial role in translation. Herein, we provide a comprehensive analysis of the stacks between different RNA components in the crystal structures of the bacterial ribosome caught at different translation stages. Analysis of tRNA||rRNA stacks reveals distinct behaviour; both the A-and E-site tRNAs exhibit unique stacking patterns with 23S rRNA bases, while P-site tRNAs stack with 16S rRNA bases. Furthermore, E-site stacks exhibit diverse face orientations and ring topologies-rare for inter-chain RNA interactions-with higher average interaction energies than A or P-site stacks. This suggests that stacking may be essential for stabilizing tRNA progression through the E-site. Additionally, mRNA||rRNA stacks reveal other geometries, which depend on the tRNA binding site, whereas 16S rRNA||23S rRNA stacks highlight the importance of specific bases in maintaining the integrity of the translational complex by linking the two rRNAs. Furthermore, tRNA||mRNA stacks exhibit distinct geometries and energetics at the E-site, indicating their significance during tRNA translocation and elimination. Overall, both A and E-sites display a more diverse distribution of inter-RNA stacks compared to the P-site. Stacking interactions in the active ribosome are not simply accidental byproducts of biochemistry but are likely invoked to compensate and support the integrity and dynamics of translation.<br />Competing Interests: Declaration of Competing Interest JFT is the President and CEO of Binary Star Research Services. BSRS had no input into the methodology or conclusions of this study and has no business interests in the specific subject of this study. The other authors claim no conflict of interest.<br /> (Copyright © 2023 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1873-4200
Volume :
305
Database :
MEDLINE
Journal :
Biophysical chemistry
Publication Type :
Academic Journal
Accession number :
38061282
Full Text :
https://doi.org/10.1016/j.bpc.2023.107144