ArticleThe Journal of biological chemistry2012
Mechanisms for defining supercoiling set point of DNA gyrase orthologs: I. A nonconserved acidic C-terminal tail modulates Escherichia coli gyrase activity.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 64 citations in OpenAlex.
- AssessingbioRxiv : the preprint server for biology · 2026Article
- Bacterial type II topoisomerases cleave DNA in a species-specific manner.Nucleic acids research · 2026Article
- Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024Article
- What's on the Other Side of the Gate: A Structural Perspective on DNA Gate Opening of Type IA and IIA DNA Topoisomerases.International journal of molecular sciences · 2023Review
- A tale of topoisomerases and the knotty genetic material in the backdrop of Plasmodium biology.Bioscience reports · 2022Review
- Two-Dimensional Gel Electrophoresis to Study the Activity of Type IIA Topoisomerases on Plasmid Replication Intermediates.Biology · 2021Article
- 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
- The pivot point arginines identified in the β-pinwheel structure of C-terminal domain from Salmonella Typhi DNA Gyrase A subunit.Scientific reports · 2020Article
- Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase.Nucleic acids research · 2020Article
- Functional interactions between gyrase subunits are optimized in a species-specific manner.The Journal of biological chemistry · 2020Article
- Cryo-EM structure of the complete E. coli DNA gyrase nucleoprotein complex.Nature communications · 2019Article
- Quinolone antibiotics.MedChemComm · 2019Review
- Supercoil Levels inMicroorganisms · 2019Article
- 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
- Hfq chaperone brings speed dating to bacterial sRNA.Wiley interdisciplinary reviews. RNA · 2018Review
- Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018Review
- Dynamic coupling between conformations and nucleotide states in DNA gyrase.Nature chemical biology · 2018Article
- Why Two? On the Role of (A-)Symmetry in Negative Supercoiling of DNA by Gyrase.International journal of molecular sciences · 2018Review
- Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
DNA topoisomerases manage chromosome supercoiling and organization in all cells. Gyrase, a prokaryotic type IIA topoisomerase, consumes ATP to introduce negative supercoils through a strand passage mechanism. All type IIA topoisomerases employ a similar set of catalytic domains for function; however, the activity and specificity of gyrase are augmented by a specialized DNA binding and wrapping element, termed the C-terminal domain (CTD), which is appended to its GyrA subunit. We have discovered that a nonconserved, acidic tail at the extreme C terminus of the Escherichia coli GyrA CTD has a dramatic and unexpected impact on gyrase function. Removal of the CTD tail enables GyrA to introduce writhe into DNA in the absence of GyrB, an activity exhibited by other GyrA orthologs, but not by wild-type E. coli GyrA. Strikingly, a "tail-less" gyrase holoenzyme is markedly impaired for DNA supercoiling capacity, but displays normal ATPase function. Our findings reveal that the E. coli GyrA tail regulates DNA wrapping by the CTD to increase the coupling efficiency between ATP turnover and supercoiling, demonstrating that CTD functions can be fine-tuned to control gyrase activity in a highly sophisticated manner.
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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.