TopR2, the Second Reverse Gyrase of Sulfolobus solfataricus, Exhibits Unusual Properties

Bizard, Anna H.; Garnier, Florence; Nadal, Marc

doi:10.1016/j.jmb.2011.03.030

Cited by 24 publications

(51 citation statements)

References 52 publications

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“…The BamHI/XhoI fragment was cloned in PET29a in-frame with a sequence coding for a histidine tag at its C terminus, producing Pet-29a-RecQ. The S. solfataricus topA gene (coding for SsTop3) was cloned without any tag by using the procedure described previously for the two reverse gyrases (30).…”

Section: Methodsmentioning

confidence: 99%

“…Recombinant S. solfataricus SSB was purified from E. coli transformed with plasmid pET28c-SSB (provided by M. F. White, University of St. Andrews, Fife, Scotland, UK) using the procedure described previously (31). Recombinant S. solfataricus SsTop3 was expressed and purified as described previously for the two reverse gyrases (30). Recombinant His-tagged E. coli topoisomerase 3 was purified as described previously (26).…”

Section: Methodsmentioning

confidence: 99%

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Synergic and Opposing Activities of Thermophilic RecQ-like Helicase and Topoisomerase 3 Proteins in Holliday Junction Processing and Replication Fork Stabilization

Valenti

Felice

Perugino

et al. 2012

Journal of Biological Chemistry

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Background: RecQ helicases and topoisomerase 3 enzymes play essential functions in all DNA activities, and their malfunctioning is associated with genomic instability. Results: A RecQ-like helicase and topoisomerase 3 from thermophilic archaea interact physically and functionally. Conclusion:The thermophilic enzymes show synergic and antagonistic activities on different DNA substrates. Significance: The results suggest a novel mechanism of modulation of RecQ-like helicases by topoisomerase 3 enzymes.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Synergic and Opposing Activities of Thermophilic RecQ-like Helicase and Topoisomerase 3 Proteins in Holliday Junction Processing and Replication Fork Stabilization

Valenti

Felice

Perugino

et al. 2012

Journal of Biological Chemistry

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“…S1). A single putative Zn finger, conserved in all RGs, is present at the N terminus (aa [11][12][13][14][15][16][17][18][19][20]; the region corresponding to the latch is longer than in most of the other RGs (aa 432 to 536), as is the insert in the H1 domain (aa 242-290).…”

Section: Resultsmentioning

confidence: 99%

“…These features make PcalRG a very robust and extreme enzyme if compared with well-characterized RGs. For instance, of the two Sulfolobus RGs, TopR2 was shown to be a very processive enzyme, with comparable positive supercoiling efficiency from 60°C up to its temperature maximum of 75°C (16). In contrast, TopR1 was found optimally active at 90°C, typically distributive, and the supercoiling level of its products was modulated by temperature.…”

Section: Discussionmentioning

confidence: 99%

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The Reverse Gyrase from Pyrobaculum calidifontis, a Novel Extremely Thermophilic DNA Topoisomerase Endowed with DNA Unwinding and Annealing Activities

Jamroze

Perugino

Valenti

et al. 2014

Journal of Biological Chemistry

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Background:The thermophilic DNA topoisomerase reverse gyrase induces DNA-positive supercoiling. Results: The novel reverse gyrase, PcalRG, is presented. Conclusion: PcalRG is the most efficient and robust reverse gyrase known, and the first inducing ATP-dependent unwinding of Holliday junctions and annealing of single-stranded oligonucleotides. Significance: PcalRG shares structural and functional features with evolutionary conserved helicase-topoisomerase complexes involved in genome stability.

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DNA topoisomerases: Advances in understanding of cellular roles and multi‐protein complexes via structure‐function analysis

Neuman²,

2021

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DNA topoisomerases, capable of manipulating DNA topology, are ubiquitous and indispensable for cellular survival due to the numerous roles they play during DNA metabolism. As we review here, current structural approaches have revealed unprecedented insights into the complex DNA‐topoisomerase interaction and strand passage mechanism, helping to advance our understanding of their activities in vivo. This has been complemented by single‐molecule techniques, which have facilitated the detailed dissection of the various topoisomerase reactions. Recent work has also revealed the importance of topoisomerase interactions with accessory proteins and other DNA‐associated proteins, supporting the idea that they often function as part of multi‐enzyme assemblies in vivo. In addition, novel topoisomerases have been identified and explored, such as topo VIII and Mini‐A. These new findings are advancing our understanding of DNA‐related processes and the vital functions topos fulfil, demonstrating their indispensability in virtually every aspect of DNA metabolism.

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TopR2, the Second Reverse Gyrase of Sulfolobus solfataricus, Exhibits Unusual Properties

Cited by 24 publications

References 52 publications

Synergic and Opposing Activities of Thermophilic RecQ-like Helicase and Topoisomerase 3 Proteins in Holliday Junction Processing and Replication Fork Stabilization

Synergic and Opposing Activities of Thermophilic RecQ-like Helicase and Topoisomerase 3 Proteins in Holliday Junction Processing and Replication Fork Stabilization

The Reverse Gyrase from Pyrobaculum calidifontis, a Novel Extremely Thermophilic DNA Topoisomerase Endowed with DNA Unwinding and Annealing Activities

DNA topoisomerases: Advances in understanding of cellular roles and multi‐protein complexes via structure‐function analysis

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