ArticleNucleic acids research2011
Guiding strand passage: DNA-induced movement of the gyrase C-terminal domains defines an early step in the supercoiling cycle.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- What makes a type IIA topoisomerase a gyrase or a Topo IV?Nucleic acids research · 2021Review
- Towards Conformation-Sensitive Inhibition of Gyrase: Implications of Mechanistic Insight for the Identification and Improvement of Inhibitors.Molecules (Basel, Switzerland) · 2021Review
- DNA Topoisomerase Inhibitors: Trapping a DNA-Cleaving Machine in Motion.Journal of molecular biology · 2019Review
- Single-nucleotide-resolution mapping of DNA gyrase cleavage sites across the Escherichia coli genome.Nucleic acids research · 2019Article
- CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage.eLife · 2018Article
- Gyrase containing a single C-terminal domain catalyzes negative supercoiling of DNA by decreasing the linking number in steps of two.Nucleic acids research · 2018Article
- Why Two? On the Role of (A-)Symmetry in Negative Supercoiling of DNA by Gyrase.International journal of molecular sciences · 2018Review
- DNA gyrase with a single catalytic tyrosine can catalyze DNA supercoiling by a nicking-closing mechanism.Nucleic acids research · 2016Article
- Structural Dynamics and Mechanochemical Coupling in DNA Gyrase.Journal of molecular biology · 2016Article
- DNA Topoisomerases.EcoSal Plus · 2015Review
- Direct control of type IIA topoisomerase activity by a chromosomally encoded regulatory protein.Genes & development · 2014Article
- The acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyrase.The Journal of biological chemistry · 2014Article
- Studying DNA-protein interactions with single-molecule Förster resonance energy transfer.Protoplasma · 2014Review
- Structural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomerase.Nucleic acids research · 2013Article
- The GyrA-box determines the geometry of DNA bound to gyrase and couples DNA binding to the nucleotide cycle.Nucleic acids research · 2012Article
- The role of Ca²⁺ in the activity of Mycobacterium tuberculosis DNA gyrase.Nucleic acids research · 2012Article
- ATP binding controls distinct structural transitions of Escherichia coli DNA gyrase in complex with DNA.Nature structural & molecular biology · 2012Article
- Potassium ions are required for nucleotide-induced closure of gyrase N-gate.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA gyrase catalyzes ATP-dependent negative supercoiling of DNA in a strand passage mechanism. A double-stranded segment of DNA, the T-segment, is passed through the gap in a transiently cleaved G-segment by coordinated closing and opening of three protein interfaces in gyrase. T-segment capture is thought to be guided by the C-terminal domains of the GyrA subunit of gyrase that wrap DNA around their perimeter and cause a DNA-crossing with a positive handedness. We show here that the C-terminal domains are in a downward-facing orientation in the absence of DNA, but swing up and rotate away from the gyrase body when DNA binds. The upward movement of the C-terminal domains is an early event in the catalytic cycle of gyrase that is triggered by binding of a G-segment, and first contacts of the DNA with the C-terminal domains, and contributes to T-segment capture and subsequent strand passage.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.