Evidence map›Paper›PMID 11087868›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Mechanism for a transcriptional activator that works at the isomerization step.

S L Dove, F W Huang, A Hochschild

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Structural basis of transcription activation.Science (New York, N.Y.) · 2016
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The transition from transcriptional initiation to elongation.Current opinion in genetics & development · 2008
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. The effects of upstream DNA on open complex formation by Escherichia coli RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  18. Article
  19. Article
  20. A regulator that inhibits transcription by targeting an intersubunit interaction of the RNA polymerase holoenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2004
    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 1 institution in 1 country.

S L DoveDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
F W Huang
A Hochschild
Harvard University · US

Funding

PROTEIN/PROTEIN INTERACTIONS IN PROKARYOTIC GENE CONTROLR01GM044025 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOCHSCHILD, ANN · 1990 to 2015
$8.1M
NIGMS NIH HHS GM44025NIGMS NIH HHS R01 GM044025
6 · The paper itself

Abstract

Transcriptional activators in prokaryotes have been shown to stimulate different steps in the initiation process including the initial binding of RNA polymerase (RNAP) to the promoter and a postbinding step known as the isomerization step. Evidence suggests that activators that affect initial binding can work by a cooperative binding mechanism by making energetically favorable contacts with RNAP, but the mechanism by which activators affect the isomerization step is unclear. A well-studied example of an activator that normally exerts its effect exclusively on the isomerization step is the bacteriophage lambda cI protein (lambdacI), which has been shown genetically to interact with the C-terminal region of the final sigma(70) subunit of RNAP. We show here that the interaction between lambdacI and final sigma can stimulate transcription even when the relevant portion of final sigma is transplanted to another subunit of RNAP. This activation depends on the ability of lambdacI to stabilize the binding of the transplanted final sigma moiety to an ectopic -35 element. Based on these and previous findings, we discuss a simple model that explains how an activator's ability to stabilize the binding of an RNAP subdomain to the DNA can account for its effect on either the initial binding of RNAP to a promoter or the isomerization step.

Indexed as

Promoter Regions, GeneticTranscription, GeneticBacteriophage lambdabeta-GalactosidaseDNA-Binding ProteinsDNA-Directed RNA PolymerasesEscherichia coliIsomerismKineticsProtein BindingRepressor ProteinsTrans-ActivatorsViral ProteinsViral Regulatory and Accessory Proteinsbeta-GalactosidaseDNA-Binding ProteinsDNA-Directed RNA Polymerasesphage repressor proteinsRepressor ProteinsTrans-ActivatorsViral ProteinsViral Regulatory and Accessory Proteins

Identifiers

PMID11087868
PMCPMC27205
OpenAlexW1990021260

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.