ArticleNucleic acids research2009
Inhibition of translesion DNA polymerase by archaeal reverse gyrase.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Regulation of DNA Topology in Archaea: State of the Art and Perspectives.Molecular microbiology · 2025Review
- How Do Thermophiles Organize Their Genomes?Microbes and environments · 2024Review
- 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
- Archaea: A Gold Mine for Topoisomerase Diversity.Frontiers in microbiology · 2021Review
- Direct observation of helicase-topoisomerase coupling within reverse gyrase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Every OGT Is Illuminated … by Fluorescent and Synchrotron Lights.International journal of molecular sciences · 2017Review
- In vivo and in vitro protein imaging in thermophilic archaea by exploiting a novel protein tag.PloS one · 2017Article
- Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein.Nucleic acids research · 2015Article
- Chromatin structure and dynamics in hot environments: architectural proteins and DNA topoisomerases of thermophilic archaea.International journal of molecular sciences · 2014Review
- Insight into the cellular involvement of the two reverse gyrases from the hyperthermophilic archaeon Sulfolobus solfataricus.BMC molecular biology · 2014Article
- 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
- Activity and regulation of archaeal DNA alkyltransferase: conserved protein involved in repair of DNA alkylation damage.The Journal of biological chemistry · 2012Article
- The archaeal topoisomerase reverse gyrase is a helix-destabilizing protein that unwinds four-way DNA junctions.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reverse gyrase is a unique DNA topoisomerase endowed with ATP-dependent positive supercoiling activity. It is typical of microorganisms living at high temperature and might play a role in maintenance of genome stability and repair. We have identified the translesion DNA polymerase SsoPolY/Dpo4 as one partner of reverse gyrase in the hyperthermophilic archaeon Sulfolobus solfataricus. We show here that in cell extracts, PolY and reverse gyrase co-immunoprecipitate with each other and with the single strand binding protein, SSB. The interaction is confirmed in vitro by far-western and Surface Plasmon Resonance. In functional assays, reverse gyrase inhibits PolY, but not the S. solfataricus B-family DNA polymerase PolB1. Mutational analysis shows that inhibition of PolY activity depends on both ATPase and topoisomerase activities of reverse gyrase, suggesting that the intact positive supercoiling activity is required for PolY inhibition. In vivo, reverse gyrase and PolY are degraded after induction of DNA damage. Inhibition by reverse gyrase and degradation might act as a double mechanism to control PolY and prevent its potentially mutagenic activity when undesired. Inhibition of a translesion polymerase by topoisomerase-induced modification of DNA structure may represent a previously unconsidered mechanism of regulation of these two-faced enzymes.
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