Evidence map›Paper›PMID 29346615›Full record

ArticleNucleic acids research2018

The RNA-splicing endonuclease from the euryarchaeaon Methanopyrus kandleri is a heterotetramer with constrained substrate specificity.

Ayano Kaneta, Kosuke Fujishima, Wataru Morikazu, Hiroyuki Hori, Akira Hirata

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  2. Article
  3. Review
  4. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  5. Review
  6. Article
  7. Review
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

5 authors at 2 institutions in 1 country.

Ayano KanetaDepartment of Materials Science and Biotechnology, Graduate School of Science and Engineering, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
Kosuke FujishimaEarth-Life Science Institute, Tokyo Institute of Technology, Meguro-ku, Tokyo 152-8550, Japan.
Wataru MorikazuDepartment of Materials Science and Biotechnology, Graduate School of Science and Engineering, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
Hiroyuki HoriDepartment of Materials Science and Biotechnology, Graduate School of Science and Engineering, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
Akira HirataDepartment of Materials Science and Biotechnology, Graduate School of Science and Engineering, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
Ehime University · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Four different types (α4, α'2, (αβ)2 and ϵ2) of RNA-splicing endonucleases (EndAs) for RNA processing are known to exist in the Archaea. Only the (αβ)2 and ϵ2 types can cleave non-canonical introns in precursor (pre)-tRNA. Both enzyme types possess an insert associated with a specific loop, allowing broad substrate specificity in the catalytic α units. Here, the hyperthermophilic euryarchaeon Methanopyrus kandleri (MKA) was predicted to harbor an (αβ)2-type EndA lacking the specific loop. To characterize MKA EndA enzymatic activity, we constructed a fusion protein derived from MKA α and β subunits (fMKA EndA). In vitro assessment demonstrated complete removal of the canonical bulge-helix-bulge (BHB) intron structure from MKA pre-tRNAAsn. However, removal of the relaxed BHB structure in MKA pre-tRNAGlu was inefficient compared to crenarchaeal (αβ)2 EndA, and the ability to process the relaxed intron within mini-helix RNA was not detected. fMKA EndA X-ray structure revealed a shape similar to that of other EndA types, with no specific loop. Mapping of EndA types and their specific loops and the tRNA gene diversity among various Archaea suggest that MKA EndA is evolutionarily related to other (αβ)2-type EndAs found in the Thaumarchaeota, Crenarchaeota and Aigarchaeota but uniquely represents constrained substrate specificity.

Indexed as

BiocatalysisCrystallography, X-RayEndoribonucleasesEuryarchaeotaEvolution, MolecularIntronsModels, MolecularProtein SubunitsRNA PrecursorsRNA, TransferSubstrate SpecificityEndoribonucleasesProtein SubunitsRNA PrecursorsRNA, Transfersplicing endonuclease

Identifiers

PMID29346615
PMCPMC5829648
OpenAlexW2783828917

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

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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.