Evidence map›Paper›PMID 28977553›Full record

ArticleNucleic acids research2017

Transcription-translation coupling: direct interactions of RNA polymerase with ribosomes and ribosomal subunits.

Haitian Fan, Adam B Conn, Preston B Williams, Stephen Diggs, Joseph Hahm, Howard B Gamper, Ya-Ming Hou, Seán E O'Leary, Yinsheng Wang, Gregor M Blaha

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.0field-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

43 citing papers in PubMed, 79 citations in OpenAlex.

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  13. Structural advances in transcription elongation.Current opinion in structural biology · 2022
    Review
  14. AnBio-protocol · 2022
    Article
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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

10 authors at 2 institutions in 1 country.

Haitian FanDepartment of Biochemistry, University of California, Riverside, CA 92521, USA.
Adam B ConnDepartment of Biochemistry, University of California, Riverside, CA 92521, USA.
Preston B WilliamsDepartment of Chemistry, University of California, Riverside, CA 92521, USA.
Stephen DiggsDepartment of Biochemistry, University of California, Riverside, CA 92521, USA.
Joseph HahmDepartment of Biochemistry, University of California, Riverside, CA 92521, USA.
Howard B GamperDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Ya-Ming HouDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Seán E O'LearyDepartment of Biochemistry, University of California, Riverside, CA 92521, USA.
Yinsheng WangDepartment of Chemistry, University of California, Riverside, CA 92521, USA.
Gregor M BlahaDepartment of Biochemistry, University of California, Riverside, CA 92521, USA.
University of California, Riverside · USThomas Jefferson University · US

Funding

AdoMet-dependent tRNA methyl transferasesR01GM114343 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2015 to 2018
$1.3M
Probes for a tRNA modification enzymeU01GM108972 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI HOU, YA-MING · 2015 to 2016
$603k
NIGMS NIH HHS R01 GM114343NIGMS NIH HHS U01 GM108972
6 · The paper itself

Abstract

In prokaryotes, RNA polymerase and ribosomes can bind concurrently to the same RNA transcript, leading to the functional coupling of transcription and translation. The interactions between RNA polymerase and ribosomes are crucial for the coordination of transcription with translation. Here, we report that RNA polymerase directly binds ribosomes and isolated large and small ribosomal subunits. RNA polymerase and ribosomes form a one-to-one complex with a micromolar dissociation constant. The formation of the complex is modulated by the conformational and functional states of RNA polymerase and the ribosome. The binding interface on the large ribosomal subunit is buried by the small subunit during protein synthesis, whereas that on the small subunit remains solvent-accessible. The RNA polymerase binding site on the ribosome includes that of the isolated small ribosomal subunit. This direct interaction between RNA polymerase and ribosomes may contribute to the coupling of transcription to translation.

Indexed as

Protein BiosynthesisTranscription, GeneticDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsKineticsModels, MolecularProtein BindingProtein DomainsRibosome SubunitsDNA-Directed RNA PolymerasesEscherichia coli Proteins

Identifiers

PMID28977553
PMCPMC5737488
OpenAlexW2747361679

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.