Evidence map›Paper›PMID 11139608›Full record

ArticleNucleic acids research2001

Characterization of Schizosaccharomyces pombe RNA triphosphatase.

Y Pei, B Schwer, S Hausmann, S Shuman

Open access · greenAbstract read
In one paragraph

Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Enzymatic Assays to Explore Viral mRNA Capping Machinery.Chembiochem : a European journal of chemical biology · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. What messenger RNA capping tells us about eukaryotic evolution.Nature reviews. Molecular cell biology · 2002
    Review
  13. Article
  14. A yeast-like mRNA capping apparatus in Plasmodium falciparum.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  15. Article
  16. Article
  17. The RNA capping machinery as an anti-infective target.Wiley interdisciplinary reviews. RNA
    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

4 authors at 1 institution in 1 country.

Y PeiMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.
B Schwer
S Hausmann
S Shuman
Kettering University · US

Funding

mRNA Capping EnzymesR01GM052470 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SCHWER, BEATE, SHUMAN, STEWART H · 1995 to 2019
$9.9M
NIGMS NIH HHS GM52470NIGMS NIH HHS R01 GM052470
6 · The paper itself

Abstract

RNA triphosphatase catalyzes the first step in mRNA cap formation which entails the cleavage of the beta-gamma phosphoanhydride bond of triphosphate-terminated RNA to yield a diphosphate end that is then capped with GMP by RNA guanylyltransferase. Here we characterize a 303 amino acid RNA triphosphatase (Pct1p) encoded by the fission yeast SCHIZOSACCHAROMYCES: pombe. Pct1p hydrolyzes the gamma phosphate of triphosphate-terminated poly(A) in the presence of magnesium. Pct1p also hydrolyzes ATP to ADP and P(i) in the presence of manganese or cobalt (K(m) = 19 microM ATP; k(cat) = 67 s(-1)). Hydrolysis of 1 mM ATP is inhibited with increasing potency by inorganic phosphate (I(0.5) = 1 mM), pyrophosphate (I(0.5) = 0.4 mM) and tripolyphosphate (I(0.5) = 30 microM). Velocity sedimentation indicates that Pct1p is a homodimer. Pct1p is biochemically and structurally similar to the catalytic domain of Saccharomyces cerevisiae RNA triphosphatase Cet1p. Mechanistic conservation between Pct1p and Cet1p is underscored by a mutational analysis of the putative metal-binding site of Pct1p. Pct1p is functional in vivo in S.cerevisiae in lieu of Cet1p, provided that it is coexpressed with the S.pombe guanylyltransferase. Pct1p and other yeast RNA triphosphatases are completely unrelated, mechanistically and structurally, to the metazoan RNA triphosphatases, suggesting an abrupt evolutionary divergence of the capping apparatus during the transition from fungal to metazoan species.

Indexed as

Acid Anhydride HydrolasesAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceAnimalsArtificial Gene FusionDiphosphatesFungal ProteinsGenetic Complementation TestHydrolysisKineticsMetalsMiceMolecular Sequence DataNucleotidyltransferasesPhosphatesAcid Anhydride HydrolasesAdenosine TriphosphateDiphosphatesFungal ProteinsguanylyltransferaseMetalsNucleotidyltransferasesPhosphatesPhosphoric Monoester HydrolasesPolyphosphatesRNA CapsRNA triphosphatasetriphosphoric acid

Identifiers

PMID11139608
PMCPMC29678
OpenAlexW2139944531

What OpenQuestion holds

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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.