Evidence map›Paper›PMID 28525600›Full record

ArticleNucleic acids research2017

A novel double kink-turn module in euryarchaeal RNase P RNAs.

Lien B Lai, Akiko Tanimoto, Stella M Lai, Wen-Yi Chen, Ila A Marathe, Eric Westhof, Vicki H Wysocki, Venkat Gopalan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Crystal structures of the archaeal RNase P protein Rpp38 in complex with RNA fragments containing a K-turn motif.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  19. Article
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

8 authors at 2 institutions in 2 countries.

Lien B LaiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Akiko TanimotoDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Stella M LaiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Wen-Yi ChenDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Ila A MaratheDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Eric WesthofUniversité de Strasbourg, Centre National de la Recherche Scientifique, Architecture et Réactivité de l'ARN, UPR9002, F-67084, Strasbourg, France.
Vicki H WysockiDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
Venkat GopalanDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA.
The Ohio State University · USCentre National de la Recherche Scientifique · FR

Funding

Dissecting functional cooperation among subunits in a catalytic ribonucleoproteinR01GM120582 · NIGMS · OHIO STATE UNIVERSITY · PI GOPALAN, VENKAT · 2016 to 2019
$1.9M
NIGMS NIH HHS R01 GM120582
6 · The paper itself

Abstract

RNase P is primarily responsible for the 5΄ maturation of transfer RNAs (tRNAs) in all domains of life. Archaeal RNase P is a ribonucleoprotein made up of one catalytic RNA and five protein cofactors including L7Ae, which is known to bind the kink-turn (K-turn), an RNA structural element that causes axial bending. However, the number and location of K-turns in archaeal RNase P RNAs (RPRs) are unclear. As part of an integrated approach, we used native mass spectrometry to assess the number of L7Ae copies that bound the RPR and site-specific hydroxyl radical-mediated footprinting to localize the K-turns. Mutagenesis of each of the putative K-turns singly or in combination decreased the number of bound L7Ae copies, and either eliminated or changed the L7Ae footprint on the mutant RPRs. In addition, our results support an unprecedented 'double K-turn' module in type A and type M archaeal RPR variants.

Indexed as

Gene Expression Regulation, ArchaealArchaeal ProteinsBase SequenceHydroxyl RadicalIsoenzymesMethanocaldococcusMethanococcusMutationNucleic Acid ConformationProtein BindingPyrococcus furiosusRibonuclease PRNA, ArchaealRNA PrecursorsRNA, TransferArchaeal ProteinsHydroxyl RadicalIsoenzymesRibonuclease PRNA, ArchaealRNA PrecursorsRNA, Transfer

Identifiers

PMID28525600
PMCPMC5499556
OpenAlexW2615068423

What OpenQuestion holds

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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.