Evidence map›Paper›PMID 22298511›Full record

ArticleNucleic acids research2012

Fidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors.

Wen-Yi Chen, Deepali Singh, Lien B Lai, Michael A Stiffler, Hue D Lai, Mark P Foster, Venkat Gopalan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  2. Review
  3. The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. From end to end: tRNA editing at 5'- and 3'-terminal positions.International journal of molecular sciences · 2014
    Review
  12. Article
  13. 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

7 authors at 1 institution in 1 country.

Wen-Yi ChenDepartment of Biochemistry, and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
Deepali Singh
Lien B Lai
Michael A Stiffler
Hue D Lai
Mark P Foster
Venkat Gopalan
The Ohio State University · US

Funding

Structure and Function in Catalytic RNP AssemblyR01GM067807 · NIGMS · OHIO STATE UNIVERSITY · PI FOSTER, MARK P. · 2004 to 2009
$1.7M
NIGMS NIH HHS GM067807NIGMS NIH HHS R01 GM067807
6 · The paper itself

Abstract

RNase P, which catalyzes tRNA 5'-maturation, typically comprises a catalytic RNase P RNA (RPR) and a varying number of RNase P proteins (RPPs): 1 in bacteria, at least 4 in archaea and 9 in eukarya. The four archaeal RPPs have eukaryotic homologs and function as heterodimers (POP5•RPP30 and RPP21•RPP29). By studying the archaeal Methanocaldococcus jannaschii RPR's cis cleavage of precursor tRNA(Gln) (pre-tRNA(Gln)), which lacks certain consensus structures/sequences needed for substrate recognition, we demonstrate that RPP21•RPP29 and POP5•RPP30 can rescue the RPR's mis-cleavage tendency independently by 4-fold and together by 25-fold, suggesting that they operate by distinct mechanisms. This synergistic and preferential shift toward correct cleavage results from the ability of archaeal RPPs to selectively increase the RPR's apparent rate of correct cleavage by 11,140-fold, compared to only 480-fold for mis-cleavage. Moreover, POP5•RPP30, like the bacterial RPP, helps normalize the RPR's rates of cleavage of non-consensus and consensus pre-tRNAs. We also show that archaeal and eukaryal RNase P, compared to their bacterial relatives, exhibit higher fidelity of 5'-maturation of pre-tRNA(Gln) and some of its mutant derivatives. Our results suggest that protein-rich RNase P variants might have evolved to support flexibility in substrate recognition while catalyzing efficient, high-fidelity 5'-processing.

Indexed as

RNA Processing, Post-TranscriptionalArchaeaArchaeal ProteinsBacteriaEukaryotaNucleic Acid ConformationRibonuclease PRNA, ArchaealRNA CleavageRNA PrecursorsRNA, Transfer, GlnArchaeal ProteinsRibonuclease PRNA, ArchaealRNA PrecursorsRNA, Transfer, Gln

Identifiers

PMID22298511
PMCPMC3378863
OpenAlexW2093308205

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.