ArticleThe Journal of biological chemistry2014
The reverse gyrase from Pyrobaculum calidifontis, a novel extremely thermophilic DNA topoisomerase endowed with DNA unwinding and annealing activities.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Machine learning prediction of bacterial optimal growth temperature from protein domain signatures reveals thermoadaptation mechanisms.BMC genomics · 2025Article
- How Do Thermophiles Organize Their Genomes?Microbes and environments · 2024Review
- IND-enzymes: a repository for hydrolytic enzymes derived from thermophilic and psychrophilic bacterial species with potential industrial usage.Extremophiles : life under extreme conditions · 2021Article
- Archaea: A Gold Mine for Topoisomerase Diversity.Frontiers in microbiology · 2021Review
- Taxonomic and functional characterization of a microbial community from a volcanic englacial ecosystem in Deception Island, Antarctica.Scientific reports · 2019Article
- Recent advances in understanding extremophiles.F1000Research · 2019Review
- Every OGT Is Illuminated … by Fluorescent and Synchrotron Lights.International journal of molecular sciences · 2017Review
- Reverse gyrase is essential for microbial growth at 95 °C.Extremophiles : life under extreme conditions · 2017Article
- In vivo and in vitro protein imaging in thermophilic archaea by exploiting a novel protein tag.PloS one · 2017Article
- RNA topoisomerase is prevalent in all domains of life and associates with polyribosomes in animals.Nucleic acids research · 2016Article
- Regulation of DNA Replication Initiation by Chromosome Structure.Journal of bacteriology · 2015Review
- Chromatin structure and dynamics in hot environments: architectural proteins and DNA topoisomerases of thermophilic archaea.International journal of molecular sciences · 2014Review
- Genome stability: recent insights in the topoisomerase reverse gyrase and thermophilic DNA alkyltransferase.Extremophiles : life under extreme conditions · 2014Review
- Reverse gyrase--recent advances and current mechanistic understanding of positive DNA supercoiling.Nucleic acids research · 2014Review
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reverse gyrase is a DNA topoisomerase specific for hyperthermophilic bacteria and archaea. It catalyzes the peculiar ATP-dependent DNA-positive supercoiling reaction and might be involved in the physiological adaptation to high growth temperature. Reverse gyrase comprises an N-terminal ATPase and a C-terminal topoisomerase domain, which cooperate in enzyme activity, but details of its mechanism of action are still not clear. We present here a functional characterization of PcalRG, a novel reverse gyrase from the archaeon Pyrobaculum calidifontis. PcalRG is the most robust and processive reverse gyrase known to date; it is active over a wide range of conditions, including temperature, ionic strength, and ATP concentration. Moreover, it holds a strong ATP-inhibited DNA cleavage activity. Most important, PcalRG is able to induce ATP-dependent unwinding of synthetic Holliday junctions and ATP-stimulated annealing of unconstrained single-stranded oligonucleotides. Combined DNA unwinding and annealing activities are typical of certain helicases, but until now were shown for no other reverse gyrase. Our results suggest for the first time that a reverse gyrase shares not only structural but also functional features with evolutionary conserved helicase-topoisomerase complexes involved in genome stability.
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