Evidence map›Paper›PMID 24990372›Full record

ArticleNucleic acids research2014

Structural dynamics of the two-component response regulator RstA in recognition of promoter DNA element.

Yi-Chuan Li, Chung-ke Chang, Chi-Fon Chang, Ya-Hsin Cheng, Pei-Ju Fang, Tsunai Yu, Sheng-Chia Chen, Yi-Ching Li, Chwan-Deng Hsiao, Tai-huang Huang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. 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
1.2field-weighted citation impact, top 19% 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, 29 citations in OpenAlex.

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  2. The response regulator BqsR/CarR controls ferrous iron (FebioRxiv : the preprint server for biology · 2025
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  4. ENcyclopedia of TRAnscription Factors in Bacteria and Archaea genomes (ENTRAF) version 2.0.Database : the journal of biological databases and curation · 2025
    Article
  5. Structural Insights into Regulation of Vibrio Virulence Gene Networks.Advances in experimental medicine and biology · 2023
    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 5 institutions in 1 country.

Yi-Chuan LiInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan, ROC Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan.
Chung-ke ChangInstitute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC.
Chi-Fon ChangGenomics Research Center, Academia Sinica, Taipei 115, Taiwan, ROC.
Ya-Hsin ChengInstitute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC.
Pei-Ju FangInstitute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC.
Tsunai YuInstitute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC.
Sheng-Chia ChenInstitute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC.
Yi-Ching LiInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan, ROC.
Chwan-Deng HsiaoInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan, ROC bmthh@ibms.sinica.edu.tw.
Tai-huang HuangInstitute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, ROC Genomics Research Center, Academia Sinica, Taipei 115, Taiwan, ROC Department of Physics, National Taiwan Normal University, Taipei 116, Taiwan, ROC bmthh@ibms.sinica.edu.tw.
Academia Sinica · TWInstitute of Molecular Biology, Academia Sinica · TWGenomics Research Center, Academia Sinica · TWInstitute of Biomedical Sciences, Academia Sinica · TWNational Taiwan Normal University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RstA/RstB system is a bacterial two-component regulatory system consisting of the membrane sensor, RstB and its cognate response regulator (RR) RstA. The RstA of Klebsiella pneumoniae (kpRstA) consists of an N-terminal receiver domain (RD, residues 1-119) and a C-terminal DNA-binding domain (DBD, residues 130-236). Phosphorylation of kpRstA induces dimerization, which allows two kpRstA DBDs to bind to a tandem repeat, called the RstA box, and regulate the expression of downstream genes. Here we report the solution and crystal structures of the free kpRstA RD, DBD and DBD/RstA box DNA complex. The structure of the kpRstA DBD/RstA box complex suggests that the two protomers interact with the RstA box in an asymmetric fashion. Equilibrium binding studies further reveal that the two protomers within the kpRstA dimer bind to the RstA box in a sequential manner. Taken together, our results suggest a binding model where dimerization of the kpRstA RDs provides the platform to allow the first kpRstA DBD protomer to anchor protein-DNA interaction, whereas the second protomer plays a key role in ensuring correct recognition of the RstA box.

Indexed as

Promoter Regions, GeneticBacterial ProteinsDNA, BacterialDNA-Binding ProteinsKlebsiella pneumoniaeModels, MolecularProtein BindingProtein MultimerizationProtein Structure, TertiaryThermodynamicsBacterial ProteinsDNA, BacterialDNA-Binding Proteins

Identifiers

PMID24990372
PMCPMC4117788
OpenAlexW2016126337

What OpenQuestion holds

Textmetadata
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.