ArticleExtremophiles : life under extreme conditions2011
Functional evaluation of four putative DNA-binding regions in Thermoanaerobacter tengcongensis reverse gyrase.
Article in Extremophiles : life under extreme conditions, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 9 citations in OpenAlex.
- Hydrogen-deuterium exchange points to inter-domain interactions in reverse gyrase that modulate conformational changes in positive DNA supercoiling.The Journal of biological chemistry · 2026Article
- Structure of reverse gyrase with a minimal latch that supports ATP-dependent positive supercoiling without specific interactions with the topoisomerase domain.Acta crystallographica. Section D, Structural biology · 2023Article
- The Evolution of Reverse Gyrase Suggests a Nonhyperthermophilic Last Universal Common Ancestor.Molecular biology and evolution · 2019Article
- 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
- The reverse gyrase from Pyrobaculum calidifontis, a novel extremely thermophilic DNA topoisomerase endowed with DNA unwinding and annealing activities.The Journal of biological chemistry · 2014Article
- Crystal structures of Thermotoga maritima reverse gyrase: inferences for the mechanism of positive DNA supercoiling.Nucleic acids research · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reverse gyrase (RG) is an ATP-dependent type I DNA topoisomerase that introduces positive supercoils into DNA in thermophiles. Four regions of RG, i.e., the N-terminal zinc-finger motif, the β-hairpin in subdomain H1, the "latch", and the C-terminal zinc-finger motif, were predicted to be involved in DNA binding previously. In this paper, the functions of these regions in the enzymatic activity were evaluated by mutational analysis of the Thermoanaerobacter tengcongensis reverse gyrase (TtRG). We demonstrated that TtRG exhibited positive-supercoiling activity only at high temperature (>50°C) and low salt concentration (~30 mM NaCl), and three of these four regions (except for the "latch") were involved in DNA binding. Notably, mutations in the "latch" and β-hairpin regions of TtRG strongly impaired the ATPase activity, while mutations in the two zinc-finger motifs dramatically affected its thermal stability besides significant impairment of the DNA-binding ability. Accordingly, all of these four regions were found to be indispensable for the positive-supercoiling activity of TtRG. Taken together, we revealed that these putative DNA-contact regions affect the enzymatic activity of RG in different ways, and provided new insights into the structure and function of RG.
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