Evidence map›Paper›PMID 33330920›Full record

ArticleNucleic acids research2021

Structural basis of sequestration of the anti-Shine-Dalgarno sequence in the Bacteroidetes ribosome.

Vikash Jha, Bappaditya Roy, Dushyant Jahagirdar, Zakkary A McNutt, Elan A Shatoff, Bethany L Boleratz, Dean E Watkins, Ralf Bundschuh, Kaustuv Basu, Joaquin Ortega and 1 more

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

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  10. Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Vikash JhaDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Bappaditya RoyDepartment of Microbiology, The Ohio State University, Columbus, OH 43210, USA.
Dushyant JahagirdarDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Zakkary A McNuttCenter for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Elan A ShatoffCenter for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Bethany L BoleratzOhio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.
Dean E WatkinsDepartment of Microbiology, The Ohio State University, Columbus, OH 43210, USA.
Ralf BundschuhCenter for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Kaustuv BasuDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Joaquin OrtegaDepartment of Anatomy and Cell Biology, McGill University, Montreal, Quebec H3A 0C7, Canada.
Kurt FredrickDepartment of Microbiology, The Ohio State University, Columbus, OH 43210, USA.
The Ohio State University · USMcGill University · CA

Funding

National Science Foundation MCB-2029502
6 · The paper itself

Abstract

Genomic studies have indicated that certain bacterial lineages such as the Bacteroidetes lack Shine-Dalgarno (SD) sequences, and yet with few exceptions ribosomes of these organisms carry the canonical anti-SD (ASD) sequence. Here, we show that ribosomes purified from Flavobacterium johnsoniae, a representative of the Bacteroidetes, fail to recognize the SD sequence of mRNA in vitro. A cryo-electron microscopy structure of the complete 70S ribosome from F. johnsoniae at 2.8 Å resolution reveals that the ASD is sequestered by ribosomal proteins bS21, bS18 and bS6, explaining the basis of ASD inhibition. The structure also uncovers a novel ribosomal protein-bL38. Remarkably, in F. johnsoniae and many other Flavobacteriia, the gene encoding bS21 contains a strong SD, unlike virtually all other genes. A subset of Flavobacteriia have an alternative ASD, and in these organisms the fully complementary sequence lies upstream of the bS21 gene, indicative of natural covariation. In other Bacteroidetes classes, strong SDs are frequently found upstream of the genes for bS21 and/or bS18. We propose that these SDs are used as regulatory elements, enabling bS21 and bS18 to translationally control their own production.

Indexed as

Peptide Chain Initiation, TranslationalRegulatory Sequences, Ribonucleic AcidAmino Acid SequenceBacteroidetesBase SequenceCodon, InitiatorCryoelectron MicroscopyCrystallography, X-RayEscherichia coliFlavobacteriumGene Expression Regulation, BacterialModels, MolecularNucleic Acid ConformationProtein BindingProtein ConformationPuromycinCodon, InitiatorPuromycinRegulatory Sequences, Ribonucleic AcidRNA, BacterialRNA, MessengerRNA, Ribosomal, 16SRNA, Ribosomal, 23SRNA, Ribosomal, 5S

Identifiers

PMID33330920
PMCPMC7797042
OpenAlexW3113080213

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.