ArticleThe Journal of biological chemistry2012
Essential functions of C terminus of Drosophila Topoisomerase IIIα in double holliday junction dissolution.
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 19 papers.
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Who cites it
19 citing papers in PubMed.
- Review
- The topoisomerase 3 zinc finger domain cooperates with the RMI1 scaffold to promote stable association of the BTR complex to recombination intermediates in the Caenorhabditis elegans germline.Nucleic acids research · 2022Article
- Mechanism of Bloom syndrome complex assembly required for double Holliday junction dissolution and genome stability.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An autoinhibitory role for the GRF zinc finger domain of DNA glycosylase NEIL3.The Journal of biological chemistry · 2020Article
- The many lives of type IA topoisomerases.The Journal of biological chemistry · 2020Review
- DNA topoisomerase IIIβ promotes cyst generation by inducing cyst wall protein gene expression inOpen biology · 2020Article
- Functional conservation of RecQ helicase BLM between humans and Drosophila melanogaster.Scientific reports · 2019Article
- The topoisomerase 3α zinc-finger domain T1 of Arabidopsis thaliana is required for targeting the enzyme activity to Holliday junction-like DNA repair intermediates.PLoS genetics · 2018Article
- Probing hyper-negatively supercoiled mini-circles with nucleases and DNA binding proteins.PloS one · 2018Article
- RMI1 and TOP3α limit meiotic CO formation through their C-terminal domains.Nucleic acids research · 2017Article
- Review
- Structural basis for suppression of hypernegative DNA supercoiling by E. coli topoisomerase I.Nucleic acids research · 2015Article
- Inhibition of Zn(II) binding type IA topoisomerases by organomercury compounds and Hg(II).PloS one · 2015Article
- Roles of type 1A topoisomerases in genome maintenance in Escherichia coli.PLoS genetics · 2014Article
- The dissolution of double Holliday junctions.Cold Spring Harbor perspectives in biology · 2014Review
- Top3α is required during the convergent migration step of double Holliday junction dissolution.PloS one · 2014Article
- Molecular mechanism of double Holliday junction dissolution.Cell & bioscience · 2014Review
- Role of replication protein A in double holliday junction dissolution mediated by the BLM-Topo IIIα-RMI1-RMI2 protein complex.The Journal of biological chemistry · 2013Article
- Improved methods for creating migratable Holliday junction substrates.Nucleic acids research · 2013Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Topoisomerase IIIα (Top3α) is an essential component of the double Holliday junction (dHJ) dissolvasome complex in metazoans, along with Blm and Rmi1/2. This important anti-recombinogenic function cannot be performed by Top3β, the other type IA topoisomerase present in metazoans. The two share a catalytic core but diverge in their tail regions. To understand this difference in function, we investigated the role of the unique C terminus of Top3α. The Drosophila C terminus contains an insert region not conserved among metazoans. This insert contributes an independent interaction with Blm, which may account for the absence of Rmi1 in Drosophila. Mutant Top3α lacking this insert maintains the ability to perform dHJ dissolution but only partially rescues a top3α null fly line, indicating an in vivo role for the insert. Truncation of the C terminus has a minimal effect on the type IA relaxation activity of Top3α; however, dHJ dissolution is greatly reduced. The Top3α C terminus was found to strongly interact with both Blm and DNA, which are critical to the dissolution reaction; these interactions are greatly reduced in the truncated enzyme. The truncation mutant also cannot rescue the viability of top3α null flies, indicating an essential in vivo role. Our data therefore suggest that the Top3α C terminus has an important role in dHJ dissolution (by providing an interaction interface for Blm and DNA) and an essential function in vivo.
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