Evidence map›Paper›PMID 21357417›Full record

ArticleThe Journal of biological chemistry2011

Activity map of the Escherichia coli RNA polymerase bridge helix.

Milija Jovanovic, Patricia C Burrows, Daniel Bose, Beatriz Cámara, Simone Wiesler, Xiaodong Zhang, Sivaramesh Wigneshweraraj, Robert O J Weinzierl, Martin Buck

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
  3. Structural basis of transcription: RNA polymerase II substrate binding and metal coordination using a free-electron laser.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Bacterial Transcription as a Target for Antibacterial Drug Development.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  14. Review
  15. CBR antimicrobials inhibit RNA polymerase via at least two bridge-helix cap-mediated effects on nucleotide addition.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

9 authors at 3 institutions in 2 countries.

Milija JovanovicDivision of Biology, Faculty of Medicine and Centre for Molecular Microbiology and Infection, Imperial College London, London SW7 2AZ, United Kindgom.
Patricia C Burrows
Daniel Bose
Beatriz Cámara
Simone Wiesler
Xiaodong Zhang
Sivaramesh Wigneshweraraj
Robert O J Weinzierl
Martin Buck
The University of Texas Health Science Center · USDivision of Molecular & Cellular Biosciences · USImperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D00862X/1Biotechnology and Biological Sciences Research Council BB/E00975/1Biotechnology and Biological Sciences Research Council BB/E023703/1Medical Research Council G0501703Wellcome Trust 084599/Z/07/Z
6 · The paper itself

Abstract

Transcription, the synthesis of RNA from a DNA template, is performed by multisubunit RNA polymerases (RNAPs) in all cellular organisms. The bridge helix (BH) is a distinct feature of all multisubunit RNAPs and makes direct interactions with several active site-associated mobile features implicated in the nucleotide addition cycle and RNA and DNA binding. Because the BH has been captured in both kinked and straight conformations in different crystals structures of RNAP, recently supported by molecular dynamics studies, it has been proposed that cycling between these conformations is an integral part of the nucleotide addition cycle. To further evaluate the role of the BH, we conducted systematic alanine scanning mutagenesis of the Escherichia coli RNAP BH to determine its contributions to activities required for transcription. Combining our data with an atomic model of E. coli RNAP, we suggest that alterations in the interactions between the BH and (i) the trigger loop, (ii) fork loop 2, and (iii) switch 2 can help explain the observed changes in RNAP functionality associated with some of the BH variants. Additionally, we show that extensive defects in E. coli RNAP functionality depend upon a single previously not studied lysine residue (Lys-781) that is strictly conserved in all bacteria. It appears that direct interactions made by the BH with other conserved features of RNAP are lost in some of the E. coli alanine substitution variants, which we infer results in conformational changes in RNAP that modify RNAP functionality.

Indexed as

AlanineAmino Acid SequenceBinding SitesDNA-Directed RNA PolymerasesEscherichia coliGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGenetic Complementation TestLysineMolecular Sequence DataMutationProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidSinorhizobium melilotiAlanineDNA-Directed RNA PolymerasesLysine

Identifiers

PMID21357417
PMCPMC3077646
OpenAlexW1970377220

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.