Kinetic insights into the temperature dependence of DNA strand cleavage and religation by topoisomerase III from the hyperthermophile Sulfolobus solfataricus.

Junhua Zhang, Bailong Pan, Zhimeng Li, Xin Sheng Zhao, Li Huang

Open access · goldAbstract read

In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

0.2field-weighted citation impact, top 44% 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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 2 citations in OpenAlex.

Direct observation of topoisomerase IA gate dynamics.Nature structural & molecular biology · 2018
Article

4 · The record

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5 · Who and what money

Authors and funding

5 authors at 4 institutions in 1 country.

Junhua ZhangState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.

Bailong PanBeijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China.

Zhimeng LiState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.

Xin Sheng ZhaoBeijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China. zhaoxs@pku.edu.cn.

Li HuangState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China. huangl@sun.im.ac.cn.

Peking University · CNChinese Academy of Sciences · CNMicrobiology Institute of Shaanxi · CNUniversity of Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

All cellular organisms encode type IA topoisomerases which catalyze DNA topological changes essential for DNA transactions. However, the kinetics of the reaction catalyzed by these enzymes remains poorly characterized. Here we measured the rapid kinetics of template binding, cleavage and religation by Sso topo III, a type IA topoisomerase from the hyperthermophilic archaeon Sulfolobus solfataricus, by using a novel FRET/PIFE-based method in a stopped-flow spectrometer. We show that Sso topo III bound the template rapidly, and the rate of binding was 2-3 orders of magnitudes higher than that of template cleavage at 25 °C. The rate of template cleavage was favored over that of template religation by the enzyme, and was more so at lower temperatures (25-55 °C). Significant template cleavage [(2.23 ± 0.11) × 10

Indexed as

DNA CleavageTemperatureBase SequenceDNA, ArchaealDNA Topoisomerases, Type IFluorescenceKineticsMagnesiumSulfolobus solfataricusTemplates, GeneticDNA, ArchaealDNA Topoisomerases, Type IMagnesium

Identifiers

PMID28710489

DOI10.1038/s41598-017-05837-5

PMCPMC5511271

OpenAlexW2735829883

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