Evidence map›Paper›PMID 33068413›Full record

ArticleNucleic acids research2020

Structural basis of Mfd-dependent transcription termination.

Jing Shi, Aijia Wen, Minxing Zhao, Sha Jin, Linlin You, Yue Shi, Shuling Dong, Xiaoting Hua, Yu Zhang, Yu Feng

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  5. Biochemical characterization ofJournal of bacteriology · 2024
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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 5 institutions in 1 country.

Jing ShiDepartment of Biophysics, Zhejiang University School of Medicine, Hangzhou 310058, China.
Aijia WenDepartment of Biophysics, Zhejiang University School of Medicine, Hangzhou 310058, China.
Minxing ZhaoDepartment of Emergency Medicine of the First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003, China.
Sha JinDepartment of Biophysics, Zhejiang University School of Medicine, Hangzhou 310058, China.
Linlin YouKey Laboratory of Synthetic Biology, CAS Center for Excellence in Molecular Plant Sciences, Shanghai Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.
Yue ShiDepartment of Pathology, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
Shuling DongSchool of Chemistry and Life Sciences, Suzhou University of Science and Technology, Suzhou 215009, China.
Xiaoting HuaDepartment of Infectious Disease, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
Yu ZhangKey Laboratory of Synthetic Biology, CAS Center for Excellence in Molecular Plant Sciences, Shanghai Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.
Yu FengDepartment of Biophysics, Zhejiang University School of Medicine, Hangzhou 310058, China.
Sir Run Run Shaw Hospital · CNChinese Academy of Sciences · CNZhejiang University · CNFirst Affiliated Hospital Zhejiang University · CNSuzhou University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mfd-dependent transcription termination plays an important role in transcription-coupled DNA repair, transcription-replication conflict resolution, and antimicrobial resistance development. Despite extensive studies, the molecular mechanism of Mfd-dependent transcription termination in bacteria remains unclear, with several long-standing puzzles. How Mfd is activated by stalled RNA polymerase (RNAP) and how activated Mfd translocates along the DNA are unknown. Here, we report the single-particle cryo-electron microscopy structures of T. thermophilus Mfd-RNAP complex with and without ATPγS. The structures reveal that Mfd undergoes profound conformational changes upon activation, contacts the RNAP β1 domain and its clamp, and pries open the RNAP clamp. These structures provide a foundation for future studies aimed at dissecting the precise mechanism of Mfd-dependent transcription termination and pave the way for rational drug design targeting Mfd for the purpose of tackling the antimicrobial resistance crisis.

Indexed as

Transcription Termination, GeneticAdenosine TriphosphateBacterial ProteinsCryoelectron MicroscopyDNA, BacterialDNA-Directed RNA PolymerasesModels, MolecularThermus thermophilusTranscription Factorsadenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphateBacterial ProteinsDNA, BacterialDNA-Directed RNA PolymerasesTranscription Factorstranscription repair coupling factor protein, Bacteria

Identifiers

PMID33068413
PMCPMC7672476
OpenAlexW3093145736

What OpenQuestion holds

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LicenceCC BY
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.