ArticleEukaryotic cell2009
A unique 45-amino-acid region in the toprim domain of Plasmodium falciparum gyrase B is essential for its activity.
Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Discovery of Potent Antimalarial Agents Targeting Plasmodium falciparum DNA Gyrase B by Integrating Computational and Experimental Approaches.Chemical biology & drug design · 2026Article
- A tale of topoisomerases and the knotty genetic material in the backdrop of Plasmodium biology.Bioscience reports · 2022Review
- Inhibitory Compounds Targeting Plasmodium falciparum Gyrase B.Antimicrobial agents and chemotherapy · 2021Article
- Synthesis of Novel Ciprofloxacin-Based Hybrid Molecules toward Potent Antimalarial Activity.ACS medicinal chemistry letters · 2020Article
- Unique features of apicoplast DNA gyrases from Toxoplasma gondii and Plasmodium falciparum.BMC bioinformatics · 2014Article
- Potent antimalarial activity of acriflavine in vitro and in vivo.ACS chemical biology · 2014Article
- Binding of two DNA molecules by type II topoisomerases for decatenation.Nucleic acids research · 2012Article
- Single-stranded DNA binding protein from human malarial parasite Plasmodium falciparum is encoded in the nucleus and targeted to the apicoplast.Nucleic acids research · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
DNA gyrase is the only topoisomerase that can introduce negative supercoils into the DNA at the cost of ATP hydrolysis. Some but not all the steps of the topoisomerization reaction are understood clearly for both eukaryotic topoII and DNA gyrase. This study is an attempt to understand whether the B subunit of DNA gyrase binds to DNA directly, which may be central to the stimulation of its ATPase activity essential for gyrase function. We have dissected the Plasmodium falciparum gyrase B (PfGyrB) subunit to identify a 45-amino-acid region in the toprim domain that is responsible for its intrinsic DNA binding activity, DNA-stimulated ATPase activity, and DNA cleavage. We find that DNA has to enter through the ATP-operated clamp of PfGyrB to gain access to the DNA binding region. Furthermore, the rate of ATP hydrolysis of PfGyrB increases significantly with increasing DNA length, suggesting a possible communication between the ATPase domain and the DNA binding region that can account for its optimal ATPase activity. These results not only highlight the mechanism of GyrB action in the deadly human parasite P. falciparum but also provide meaningful insights into the current mechanistic model of DNA transport by gyrase during the topoisomerization reaction.
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Registered trials
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