Evidence map›Paper›PMID 19666603›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Structure of the C-terminal domain of transcription factor IIB from Trypanosoma brucei.

B Syed Ibrahim, Nalini Kanneganti, Gabrielle E Rieckhof, Anish Das, Douglas V Laurents, Jennifer B Palenchar, Vivian Bellofatto, David A Wah

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

8 authors at 4 institutions in 2 countries.

B Syed IbrahimPublic Health Research Institute and Department of Biochemistry and Molecular Biology, New Jersey Medical School, University of Medicine & Dentistry of New Jersey, 225 Warren Street, Newark, NJ 07103, USA.
Nalini Kanneganti
Gabrielle E Rieckhof
Anish Das
Douglas V Laurents
Jennifer B Palenchar
Vivian Bellofatto
David A Wah
Rutgers, The State University of New Jersey · USInstituto de Química Física Blas Cabrera · ESRockefeller University · USVillanova University · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
TRYPANOSOME MRNA SYNTHESIS BY GENE TRANSFERR01AI029478 · NIAID · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI BELLOFATTO, VIVIAN · 1991 to 2010
$4.6M
NIAID NIH HHS AI-29478NIAID NIH HHS R01 AI029478NIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

In trypanosomes, the production of mRNA relies on the synthesis of the spliced leader (SL) RNA. Expression of the SL RNA is initiated at the only known RNA polymerase II promoter in these parasites. In the pathogenic trypanosome, Trypanosoma brucei, transcription factor IIB (tTFIIB) is essential for SL RNA gene transcription and cell viability, but has a highly divergent primary sequence in comparison to TFIIB in well-studied eukaryotes. Here we describe the 2.3 A resolution structure of the C-terminal domain of tTFIIB (tTFIIB(C)). The tTFIIB(C) structure consists of 2 closely packed helical modules followed by a C-terminal extension of 32 aa. Using the structure as a guide, alanine substitutions of basic residues in regions analogous to functionally important regions of the well-studied eukaryotic TFIIB support conservation of a general mechanism of TFIIB function in eukaryotes. Strikingly, tTFIIB(C) contains additional loops and helices, and, in contrast to the highly basic DNA binding surface of human TFIIB, contains a neutral surface in the corresponding region. These attributes probably mediate trypanosome-specific interactions and have implications for the apparent bidirectional transcription by RNA polymerase II in protein-encoding gene expression in these organisms.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsDNAHumansModels, MolecularMolecular Sequence DataMutant ProteinsProtein BindingProtein FoldingProtein StabilityProtein Structure, TertiaryStatic ElectricityStructural Homology, ProteinTranscription Factor TFIIBTranscription, GeneticDNAMutant ProteinsTranscription Factor TFIIB

Identifiers

PMID19666603
PMCPMC2726365
OpenAlexW2121167394

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.