ArticleJournal of molecular biology2013
Distinct regions of the Escherichia coli ParC C-terminal domain are required for substrate discrimination by topoisomerase IV.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Mechanism of negative supercoil relaxation by Topoisomerase IV.Nucleic acids research · 2026Article
- Different propensities for gate opening in gyrases and topoisomerase IV.Nucleic acids research · 2025Article
- Structural and functional insights into the T-even type bacteriophage topoisomerase II.Nature communications · 2024Article
- Telling Your Right Hand from Your Left: The Effects of DNA Supercoil Handedness on the Actions of Type II Topoisomerases.International journal of molecular sciences · 2023Review
- Basis for the discrimination of supercoil handedness during DNA cleavage by human and bacterial type II topoisomerases.Nucleic acids research · 2023Article
- Control of topoisomerase II activity and chemotherapeutic inhibition by TCA cycle metabolites.Cell chemical biology · 2022Article
- Article
- What makes a type IIA topoisomerase a gyrase or a Topo IV?Nucleic acids research · 2021Review
- Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase.Nucleic acids research · 2020Article
- DNA Topoisomerase Inhibitors: Trapping a DNA-Cleaving Machine in Motion.Journal of molecular biology · 2019Review
- Topoisomerase VI senses and exploits both DNA crossings and bends to facilitate strand passage.eLife · 2018Article
- The Localization and Action of Topoisomerase IV in Escherichia coli Chromosome Segregation Is Coordinated by the SMC Complex, MukBEF.Cell reports · 2015Article
- Article
- Structural basis for the MukB-topoisomerase IV interaction and its functional implications in vivo.The EMBO journal · 2013Article
- Article
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3 authors at 2 institutions in 1 country.
Funding
Abstract
Type IIA DNA topoisomerases are essential enzymes that use ATP to maintain chromosome supercoiling and remove links between sister chromosomes. In Escherichia coli, the type IIA topoisomerase topo IV rapidly removes positive supercoils and catenanes from DNA but is significantly slower when confronted with negatively supercoiled substrates. The ability of topo IV to discriminate between positively and negatively supercoiled DNA requires the C-terminal domain (CTD) of one of its two subunits, ParC. To determine how the ParC CTD might assist with substrate discrimination, we identified potential DNA interacting residues on the surface of the CTD, mutated these residues, and tested their effect on both topo IV enzymatic activity and DNA binding by the isolated domain. Surprisingly, different regions of the ParC CTD do not bind DNA equivalently, nor contribute equally to the action of topo IV on different types of DNA substrates. Moreover, we find that the CTD contains an autorepressive element that inhibits activity on negatively supercoiled and catenated substrates, as well as a distinct region that aids in bending the DNA duplex that tracks through the enzyme's nucleolytic center. Our data demonstrate that the CTD is essential for proper engagement of both gate and transfer segment DNAs, reconciling different models to explain how topo IV discriminates between distinct DNAs topologies.
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