Evidence map›Paper›PMID 22923611›Full record

ArticleThe Journal of biological chemistry2012

New insights into the mechanism of initial transcription: the T7 RNA polymerase mutant P266L transitions to elongation at longer RNA lengths than wild type.

Luis E Ramírez-Tapia, Craig T Martin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Biomolecular NMR assignments · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Frontiers in microbiology · 2024
    Article
  11. Understanding the impact ofFrontiers in molecular biosciences · 2024
    Review
  12. Article
  13. Article
  14. A T7 RNA Polymerase Mutant Enhances the Yield of 5'-Thienoguanosine-Initiated RNAs.Chembiochem : a European journal of chemical biology · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
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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

2 authors at 1 institution in 1 country.

Luis E Ramírez-TapiaDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Craig T Martin
University of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
INITIATION OF TRANSCRIPTION BY T7 RNA POLYMERASER01GM055002 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI MARTIN, CRAIG T · 1997 to 2012
$2.3M
NIGMS NIH HHS 1R01 GM55002NIGMS NIH HHS R01 GM055002NIGMS NIH HHS T32 GM008515NIGMS NIH HHS T32 GM08515
6 · The paper itself

Abstract

RNA polymerases undergo substantial structural and functional changes in transitioning from sequence-specific initial transcription to stable and relatively sequence-independent elongation. Initially, transcribing complexes are characteristically unstable, yielding short abortive products on the path to elongation. However, protein mutations have been isolated in RNA polymerases that dramatically reduce abortive instability. Understanding these mutations is essential to understanding the energetics of initial transcription and promoter clearance. We demonstrate here that the P266L point mutation in T7 RNA polymerase, which shows dramatically reduced abortive cycling, also transitions to elongation later, i.e. at longer lengths of RNA. These two properties of the mutant are not necessarily coupled, but rather we propose that they both derive from a weakening of the barrier to RNA-DNA hybrid-driven rotation of the promoter binding N-terminal platform, a motion necessary to achieve programmatically timed release of promoter contacts in the transition to elongation. Parallels in the multisubunit RNA polymerases are discussed.

Indexed as

Amino Acid SubstitutionTranscription, GeneticBacteriophage T7DNA-Directed RNA PolymerasesFluorescence PolarizationKineticsModels, MolecularMutagenesis, Site-DirectedPromoter Regions, GeneticProtein BindingProtein ConformationProteolysisTrypsinViral Proteinsbacteriophage T7 RNA polymeraseDNA-Directed RNA PolymerasesTrypsinViral Proteins

Identifiers

PMID22923611
PMCPMC3481332
OpenAlexW2004945089

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.