Evidence map›Paper›PMID 9811739›Full record

ArticleJournal of virology1998

The LEF-4 subunit of baculovirus RNA polymerase has RNA 5'-triphosphatase and ATPase activities.

J Jin, W Dong, L A Guarino

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Responses of the Housefly,Frontiers in microbiology · 2017
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Baculovirus: molecular insights on their diversity and conservation.International journal of evolutionary biology · 2011
    Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. What messenger RNA capping tells us about eukaryotic evolution.Nature reviews. Molecular cell biology · 2002
    Review
  20. 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

3 authors at 2 institutions in 2 countries.

J JinDepartments of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128, USA.
W Dong
L A Guarino
Institute of Entomology · CZInstitute of Molecular Biology and Biophysics · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The baculovirus Autographa californica nuclear polyhedrosis virus encodes a DNA-dependent RNA polymerase that is required for transcription of viral late genes. This polymerase is composed of four equimolar subunits, LEF-8, LEF-4, LEF-9, and p47. The LEF-4 subunit has guanylyltransferase activity, suggesting that baculoviruses may encode a full complement of capping enzymes. Here we show that LEF-4 is a bifunctional enzyme that hydrolyzes the gamma phosphates of triphosphate-terminated RNA and also hydrolyzes ATP and GTP to the respective diphosphate forms. Alanine substitution of five residues previously shown to be essential for vaccinia virus RNA triphosphatase activity inactivated the triphosphatase component of LEF-4 but not the guanylyltransferase domain. Conversely, mutation of the invariant lysine in the guanylyltransferase domain abolished the guanylyltransferase activity without affecting triphosphatase function. We also investigated the effects of substituting phenylalanine for leucine at position 105, a mutation that results in a virus that is temperature sensitive for late gene expression. We found that this mutation had no significant effect on the ATPase or guanylyltransferase activity of LEF-4 but resulted in a modest decrease in RNA triphosphatase activity.

Indexed as

Acid Anhydride HydrolasesAdenosine TriphosphatasesAmino Acid SequenceAmino Acid SubstitutionAnimalsBase SequenceCell LineDNA-Directed RNA PolymerasesDNA PrimersEnzyme StabilityGene ExpressionGenes, ViralMolecular Sequence DataMutagenesis, Site-DirectedNucleopolyhedrovirusesProtein ConformationAcid Anhydride HydrolasesAdenosine TriphosphatasesDNA-Directed RNA PolymerasesDNA Primerslate expression factor 4, baculovirusRNA triphosphataseViral Proteins

Identifiers

PMID9811739
PMCPMC110520
OpenAlexW2126557763

What OpenQuestion holds

Textmetadata
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.