Evidence map›Paper›PMID 36660825›Full record

ArticleNucleic acids research2023

Rare ribosomal RNA sequences from archaea stabilize the bacterial ribosome.

Amos J Nissley, Petar I Penev, Zoe L Watson, Jillian F Banfield, Jamie H D Cate

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 21 citations in OpenAlex.

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  8. RNA language models predict mutations that improve RNA function.bioRxiv : the preprint server for biology · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 1 country.

Amos J NissleyDepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.ORCID 0000-0003-4829-5373
Petar I PenevInnovative Genomics Institute, University of California, Berkeley, Berkeley, CA 94720, USA.ORCID 0000-0002-9027-3824
Zoe L WatsonCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA 94720, USA.ORCID 0000-0002-4877-7914
Jillian F BanfieldInnovative Genomics Institute, University of California, Berkeley, Berkeley, CA 94720, USA.ORCID 0000-0001-8203-8771
Jamie H D CateDepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA.ORCID 0000-0001-5965-7902
QB3 · USInnovative Genomics Institute · USPlanetary Science Institute · USUniversity of California, Berkeley · US

Funding

Univ of Calif Berkeley Chemistry-Biology Interface ProgramT32GM066698 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CHANG, CHRISTOPHER J., FRANCIS, MATTHEW B · 2004 to 2023
$7.5M
NIGMS NIH HHS T32 GM066698
6 · The paper itself

Abstract

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.

Indexed as

Peptidyl TransferasesRNA, RibosomalArchaeaBacteriaBase SequenceBinding SitesCytidineEscherichia coliRibosomesRNA, BacterialRNA, Ribosomal, 23SUridineCytidinePeptidyl TransferasesRNA, BacterialRNA, RibosomalRNA, Ribosomal, 23SUridine

Identifiers

PMID36660825
PMCPMC9976906
OpenAlexW4317528980

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.