Rare ribosomal RNA sequences from archaea stabilize the bacterial ribosome.


Journal

Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011

Informations de publication

Date de publication:
28 02 2023
Historique:
accepted: 28 12 2022
revised: 15 12 2022
received: 09 11 2022
pubmed: 21 1 2023
medline: 4 3 2023
entrez: 20 1 2023
Statut: ppublish

Résumé

The ribosome serves as the universally conserved translator of the genetic code into proteins and supports life across diverse temperatures ranging from below freezing to above 120°C. Ribosomes are capable of functioning across this wide range of temperatures even though the catalytic site for peptide bond formation, the peptidyl transferase center, is nearly universally conserved. Here we find that Thermoproteota, a phylum of thermophilic Archaea, substitute cytidine for uridine at large subunit rRNA positions 2554 and 2555 (Escherichia coli numbering) in the A loop, immediately adjacent to the binding site for the 3'-end of A-site tRNA. We show by cryo-EM that E. coli ribosomes with uridine to cytidine mutations at these positions retain the proper fold and post-transcriptional modification of the A loop. Additionally, these mutations do not affect cellular growth, protect the large ribosomal subunit from thermal denaturation, and increase the mutational robustness of nucleotides in the peptidyl transferase center. This work identifies sequence variation across archaeal ribosomes in the peptidyl transferase center that likely confers stabilization of the ribosome at high temperatures and develops a stable mutant bacterial ribosome that can act as a scaffold for future ribosome engineering efforts.

Identifiants

pubmed: 36660825
pii: 6993852
doi: 10.1093/nar/gkac1273
pmc: PMC9976906
doi:

Substances chimiques

RNA, Ribosomal 0
Peptidyl Transferases EC 2.3.2.12
Uridine WHI7HQ7H85
Cytidine 5CSZ8459RP
RNA, Ribosomal, 23S 0
RNA, Bacterial 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

1880-1894

Subventions

Organisme : NIGMS NIH HHS
ID : T32 GM066698
Pays : United States

Informations de copyright

© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

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Auteurs

Amos J Nissley (AJ)

Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.

Petar I Penev (PI)

Innovative Genomics Institute, University of California, Berkeley, Berkeley, CA 94720, USA.

Zoe L Watson (ZL)

California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA.

Jillian F Banfield (JF)

Innovative Genomics Institute, University of California, Berkeley, Berkeley, CA 94720, USA.
Earth and Planetary Science, University of California, Berkeley, Berkeley, CA 94720, USA.
Environmental Science, University of California, Berkeley, Berkeley, CA 94720, USA.

Jamie H D Cate (JHD)

Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.
Innovative Genomics Institute, University of California, Berkeley, Berkeley, CA 94720, USA.
California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA.
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.

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