Evidence map›Paper›PMID 25646438›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural basis for transcription reactivation by RapA.

Bin Liu, Yuhong Zuo, Thomas A Steitz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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
4.4field-weighted citation impact, top 5% 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, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Recycling of bacterial RNA polymerase by the Swi2/Snf2 ATPase RapA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Recycling of Bacterial RNA Polymerase by the Swi2/Snf2 ATPase RapA.bioRxiv : the preprint server for biology · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

3 authors at 1 institution in 2 countries.

Bin LiuDepartment of Molecular Biophysics and Biochemistry.
Yuhong ZuoDepartment of Molecular Biophysics and Biochemistry.
Thomas A SteitzDepartment of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, and Department of Chemistry, Yale University, New Haven, CT 06520 thomas.steitz@yale.edu.
Institute of Molecular Biology and Biophysics · RU

Funding

Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
STRUCTURES OF DNA POLYMERASES AND FUNCTIONAL COMPLEXESR01GM057510 · NIGMS · YALE UNIVERSITY · PI STEITZ, THOMAS ARTHUR · 1998 to 2013
$4.5M
Howard Hughes Medical InstituteNIGMS NIH HHS GM57510NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM057510
6 · The paper itself

Abstract

RNA polymerase (RNAP) loses activity during transcription as it stalls at various inactive states due to erratic translocation. Reactivation of these stalled RNAPs is essential for efficient RNA synthesis. Here we report a 4.7-Å resolution crystal structure of the Escherichia coli RNAP core enzyme in complex with ATPase RapA that is involved in reactivating stalled RNAPs. The structure reveals that RapA binds at the RNA exit channel of the RNAP and makes the channel unable to accommodate the formation of an RNA hairpin. The orientation of RapA on the RNAP core complex suggests that RapA uses its ATPase activity to propel backward translocation of RNAP along the DNA template in an elongation complex. This structure provides insights into the reactivation of stalled RNA polymerases and helps support ATP-driven backward translocation as a general mechanism for transcriptional regulation.

Indexed as

Crystallography, X-RayDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsModels, MolecularTranscription, GeneticDNA-Directed RNA PolymerasesEscherichia coli ProteinsRapA protein, E colibacktranslocationDNA translocaseRapARNA polymerasetranscription

Identifiers

PMID25646438
PMCPMC4343176
OpenAlexW2164123407

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.