Essential Functions of C Terminus of Drosophila Topoisomerase IIIα in Double Holliday Junction Dissolution

Chen, Stefanie H.; Wu, Chung-Hsuan; Plank, Jody L.; Hsieh, Tao-shih

doi:10.1074/jbc.m112.363044

Cited by 26 publications

(35 citation statements)

References 31 publications

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“…Interestingly, the fruit fly Drosophila melanogaster possesses neither a RMI1 nor RMI2 ortholog. Thus, dHJ dissolution in that organism may be mediated by the Blm-Topo III␣ complex (8,31). Consistent with this premise, it has been shown that RPA enhances dHJ dissolution catalyzed by the D. melanogaster Blm-Topo III␣ pair.…”

Section: Discussionsupporting

confidence: 64%

Role of Replication Protein A in Double Holliday Junction Dissolution Mediated by the BLM-Topo IIIα-RMI1-RMI2 Protein Complex

Xue

Raynard²,

Busygina³

et al. 2013

Journal of Biological Chemistry

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Background:The BTR complex, consisting of the BLM helicase, topoisomerase III␣, RMI1, and RMI2, dissolves the double Holliday junction (dHJ) to yield non-crossover products exclusively. Results: RPA physically interacts with RMI1 and stimulates dHJ dissolution. Conclusion: RPA-RMI1 interaction is required for efficient dHJ dissolution. Significance: RPA, through an interaction with RMI1, is essential for the functional integrity of the BTR dHJ dissolvasome.

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Section: Discussionsupporting

confidence: 64%

Role of Replication Protein A in Double Holliday Junction Dissolution Mediated by the BLM-Topo IIIα-RMI1-RMI2 Protein Complex

Xue

Raynard²,

Busygina³

et al. 2013

Journal of Biological Chemistry

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“…In this multienzyme complex, the activities of the RecQ helicase and TOP3 coordinate with each other to catalyze the dissolution of double Holliday junctions, which proceeds by the migration of the junctions towards each other until they merge to form a hemi-catenated structure that is processed by TOP3 (86). In addition to its role during the unlinking of this hemicatenane, TOP3 also assists the convergent branch migration reaction primarily driven by the ATP-dependent helicase activity of Rqh1/Sgs1/BLM (87)(88)(89). The mechanism by which TOP3 manipulates DNA topology during the convergent branch migration is still not clear, although it seems likely that the activity of the RecQ helicase specifically enables TOP3 to efficiently release the torsional stress associated with convergent branch migration (90).…”

Section: Synergy With Other Enzymesmentioning

confidence: 99%

The many lives of type IA topoisomerases

Bizard

Hickson

2020

Journal of Biological Chemistry

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The double helical structure of genomic DNA is both elegant and functional in that it serves both to protect vulnerable DNA bases and to facilitate DNA replication and compaction. However, these design advantages come at the cost of having to evolve and maintain a cellular machinery that can manipulate a long polymeric molecule that readily becomes topologically entangled whenever it has to open for translation, replication, or repair. If such a machinery fails to eliminate detrimental topological entanglements, utilization of the information stored in the DNA double helix is compromised. As a consequence, the use of Bform DNA as the carrier of genetic information must have co-evolved with a means to manipulate its complex topology. This duty is performed by DNA topoisomerases, which therefore are, unsurprisingly, ubiquitous in all kingdoms of life. In this review, we focus on how DNA topoisomerases catalyze their impressive range of DNA-conjuring tricks, with a particular emphasis on DNA topoisomerase III (TOP3). Once thought to be the most unremarkable of topoisomerases, the many lives of these type IA topoisomerases are now being progressively revealed. This research interest is driven by a realization that their substrate versatility and their ability to engage in intimate collaborations with translocases and other DNA-processing enzymes are far more extensive and impressive than was thought hitherto. This, coupled with the recent associations of TOP3s with developmental and neurological pathologies in humans, is clearly making us reconsider their undeserved reputation as being unexceptional enzymes.

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“…Finally, rmi1 is epistatic to top3, and the slow growth phenotype of Drmi1 strains can be suppressed by mutations in the SGS1 gene (Chang et al 2005;Mullen et al 2005). Rmi1 is a conserved protein, being present in nearly all eukaryotes although no ortholog has been found in D. melanogaster (Yin et al 2005;Chen et al 2012). As with TopoIIIa, Rmi1 homologs are essential in S. pombe, A. thaliana, and mice (Chang et al 2005;Hartung et al 2008;Chen et al 2011;Guiraldelli et al 2013).…”

Section: Dissolution Of Double Holliday Junctionsmentioning

confidence: 99%