Evidence map›Paper›PMID 15572698›Full record

ArticleMolecular and cellular biology2004

Amino acid substitutions in yeast TFIIF confer upstream shifts in transcription initiation and altered interaction with RNA polymerase II.

Mohamed A Ghazy, Seth A Brodie, Michelle L Ammerman, Lynn M Ziegler, Alfred S Ponticelli

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

42 citing papers in PubMed, 63 citations in OpenAlex.

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  14. Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015
    Review
  15. Article
  16. Article
  17. Transcription factors IIS and IIF enhance transcription efficiency by differentially modifying RNA polymerase pausing dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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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 1 institution in 1 country.

Mohamed A GhazyDepartment of Biochemistry, School of Medicine and Biomedical Sciences, State University of New York, Buffalo, NY 14214-3000, USA.
Seth A Brodie
Michelle L Ammerman
Lynn M Ziegler
Alfred S Ponticelli
State University of New York · US

Funding

Molecular Mechanisms of RNAPII TranscriptionR01GM051124 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI PONTICELLI, ALFRED S · 2000 to 2009
$1.9M
GENETIC AND BIOCHEMICAL ANALYSIS OF YEAST TFIIBR29GM051124 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI PONTICELLI, ALFRED S · 1993 to 1997
–
NIGMS NIH HHS GM 51124NIGMS NIH HHS R01 GM051124NIGMS NIH HHS R29 GM051124
6 · The paper itself

Abstract

Transcription factor IIF (TFIIF) is required for transcription of protein-encoding genes by eukaryotic RNA polymerase II. In contrast to numerous studies establishing a role for higher eukaryotic TFIIF in multiple steps of the transcription cycle, relatively little has been reported regarding the functions of TFIIF in the yeast Saccharomyces cerevisiae. In this study, site-directed mutagenesis, plasmid shuffle complementation assays, and primer extension analyses were employed to probe the functional domains of the S. cerevisiae TFIIF subunits Tfg1 and Tfg2. Analyses of 35 Tfg1 alanine substitution mutants and 19 Tfg2 substitution mutants identified 5 mutants exhibiting altered properties in vivo. Primer extension analyses revealed that the conditional growth properties exhibited by the tfg1-E346A, tfg1-W350A, and tfg2-L59K mutants were associated with pronounced upstream shifts in transcription initiation in vivo. Analyses of double mutant strains demonstrated functional interactions between the Tfg1 mutations and mutations in Tfg2, TFIIB, and RNA polymerase II. Importantly, biochemical results demonstrated an altered interaction between mutant TFIIF protein and RNA polymerase II. These results provide direct evidence for the involvement of S. cerevisiae TFIIF in the mechanism of transcription start site utilization and support the view that a TFIIF-RNA polymerase II interaction is a determinant in this process.

Indexed as

Transcription, GeneticAlanineAmino Acid SequenceAmino Acid SubstitutionElectrophoretic Mobility Shift AssayGenetic Complementation TestImmunoblottingMolecular Sequence DataMutagenesis, Site-DirectedPlasmidsProtein Structure, TertiaryRNA Polymerase IISaccharomyces cerevisiaeSequence Homology, Amino AcidStructure-Activity RelationshipTranscription Factors, TFIIAlanineRNA Polymerase IITranscription Factors, TFIItranscription factor TFIIF

Identifiers

PMID15572698
PMCPMC533996
OpenAlexW2119741754

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.