Evidence map›Paper›PMID 11604518›Full record

ArticleMolecular and cellular biology2001

A truncation mutant of the 95-kilodalton subunit of transcription factor IIIC reveals asymmetry in Ty3 integration.

M Aye, S L Dildine, J A Claypool, S Jourdain, S B Sandmeyer

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2001. 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
1.3field-weighted citation impact, top 22% 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, 34 citations in OpenAlex.

  1. Article
  2. Review
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  9. Article
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  12. Article
  13. Targeted gene insertion for molecular medicine.Journal of molecular medicine (Berlin, Germany) · 2008
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Integration by design.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Review
  19. Controlling integration specificity of a yeast retrotransposon.Proceedings of the National Academy of Sciences of the United States of America · 2003
    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

5 authors at 2 institutions in 2 countries.

M AyeDepartment of Biological Chemistry, University of California, Irvine, 92697, USA.
S L Dildine
J A Claypool
S Jourdain
S B Sandmeyer
University of California, Irvine · USCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

Ty3 Viruslike Particle Morphogenesis and Host InteractionsR01GM033281 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI SANDMEYER, SUZANNE · 1985 to 2013
$4.7M
SYNTHESIS AND STRUCTURE OF BIOLOGICAL MACROMOLECULEST32GM007311 · NIGMS · UNIVERSITY OF CALIFORNIA IRVINE · PI OSBORNE, TIMOTHY F · 1985 to 2004
$1.6M
NIGMS NIH HHS GM07311-24NIGMS NIH HHS GM33281NIGMS NIH HHS R01 GM033281NIGMS NIH HHS T32 GM007311
6 · The paper itself

Abstract

Position-specific integration of the retroviruslike element Ty3 near the transcription initiation sites of tRNA genes requires transcription factors IIIB and IIIC (TFIIIB and TFIIIC). Using a genetic screen, we isolated a mutant with a truncated 95-kDa subunit of TFIIIC (TFIIIC95) that reduced the apparent retrotransposition of Ty3 into a plasmid-borne target site between two divergently transcribed tRNA genes. Although TFIIIC95 is conserved and essential, no defect in growth or transcription of tRNAs was detected in the mutant. Steps of the Ty3 life cycle, such as protein expression, proteolytic processing, viruslike particle formation, and reverse transcription, were not affected by the mutation. However, Ty3 integration into a divergent tDNA target occurred exclusively in one orientation in the mutant strain. Investigation of this orientation bias showed that TFIIIC95 and Ty3 integrase interacted in two-hybrid and glutathione S-transferase pulldown assays and that interaction with the mutant TFIIIC95 protein was attenuated. The orientation bias observed here suggests that even for wild-type Ty3, the protein complexes associated with the long terminal repeats are not equivalent in vivo.

Indexed as

RetroelementsIntegrasesMutagenesisMutagenesis, InsertionalPhenotypeRNA Polymerase IIISaccharomyces cerevisiaeTranscription Factors, TFIIITranscription Factor TFIIICTranscription, GeneticIntegrasesRetroelementsRNA Polymerase IIITranscription Factors, TFIIITranscription Factor TFIIIC

Identifiers

PMID11604518
PMCPMC99953
OpenAlexW1983426450

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.