Evidence map›Paper›PMID 30544248›Full record

ArticleNucleic acids research2019

Crystal structures of HpSoj-DNA complexes and the nucleoid-adaptor complex formation in chromosome segregation.

Chen-Hsi Chu, Cheng-Yi Yen, Bo-Wei Chen, Min-Guan Lin, Lyu-Han Wang, Kai-Zhi Tang, Chwan-Deng Hsiao, Yuh-Ju Sun

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

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  9. Insights into the Orchestration of Gene Transcription Regulators inInternational journal of molecular sciences · 2022
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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

8 authors at 2 institutions in 1 country.

Chen-Hsi ChuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan.
Cheng-Yi YenInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan.
Bo-Wei ChenInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Min-Guan LinInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Lyu-Han WangInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan.
Kai-Zhi TangInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan.
Chwan-Deng HsiaoInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Yuh-Ju SunInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300, Taiwan.
National Tsing Hua University · TWInstitute of Molecular Biology, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ParABS, an important DNA partitioning process in chromosome segregation, includes ParA (an ATPase), ParB (a parS binding protein) and parS (a centromere-like DNA). The homologous proteins of ParA and ParB in Helicobacter pylori are HpSoj and HpSpo0J, respectively. We analyzed the ATPase activity of HpSoj and found that it is enhanced by both DNA and HpSpo0J. Crystal structures of HpSoj and its DNA complexes revealed a typical ATPase fold and that it is dimeric. DNA binding by HpSoj is promoted by ATP. The HpSoj-ATP-DNA complex non-specifically binds DNA through a continuous basic binding patch formed by lysine residues, with a single DNA-binding site. This complex exhibits a DNA-binding adept state with an active ATP-bound conformation, whereas the HpSoj-ADP-DNA complex may represent a transient DNA-bound state. Based on structural comparisons, HpSoj exhibits a similar DNA binding surface to the bacterial ParA superfamily, but the archaeal ParA superfamily exhibits distinct non-specific DNA-binding via two DNA-binding sites. We detected the HpSpo0J-HpSoj-DNA complex by electron microscopy and show that this nucleoid-adaptor complex (NAC) is formed through HpSoj and HpSpo0J interaction and parS DNA binding. NAC formation is promoted by HpSoj participation and specific parS DNA facilitation.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsBinding SitesCentromereChromosomes, BacterialChromosome SegregationCrystallography, X-RayDNADNA-Binding ProteinsHelicobacter pyloriAdenosine TriphosphatasesBacterial ProteinsDNADNA-Binding Proteins

Identifiers

PMID30544248
PMCPMC6393308
OpenAlexW2905553943

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Registered trials

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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.