Abstract
DNA Topoisomerase IIα (Topo IIα) is a ubiquitous enzyme in eukaryotes that performs the strand passage reaction where a double helix of DNA is passed through a second double helix. This unique reaction is critical for numerous cellular processes. However, the enzyme also possesses a C-terminal domain (CTD) that is largely dispensable for the strand passage reaction but is nevertheless important for the fidelity of cell division. Recent studies have expanded our understanding of the roles of the Topo IIα CTD, in particular in mitotic mechanisms where the CTD is modified by Small Ubiquitin-like Modifier (SUMO), which in turn provides binding sites for key regulators of mitosis.
Highlights
In this review, we summarize recent studies that have revealed insight into the non-catalytic functions of the Topo IIα C-terminal domain (CTD)
We summarize recent studies that have revealed insight into the non-catalytic functions of the Topo IIα CTD
The CTD of Topo IIα has been shown to be dispensable for the strand passage reaction [3,4], but evidence has revealed that the CTD is crucial for the fidelity of chromosome segregation in yeast, human cells, and Xenopus egg extract (XEE) [5,6,7]
Summary
We summarize recent studies that have revealed insight into the non-catalytic functions of the Topo IIα CTD. The CTD of Topo IIα has been shown to be dispensable for the strand passage reaction [3,4], but evidence has revealed that the CTD is crucial for the fidelity of chromosome segregation in yeast, human cells, and Xenopus egg extract (XEE) [5,6,7]. This led to the hypothesis that the CTD has fundamental conserved functions independent of the strand passage reaction that are required for accurate genome transmission. Ca-ttcehrmdinoaml daionmsaianb(oCvTeD).; gCr-etye)rhmaisnnaolt dbeoemnacirnyst(aCliTzDed;. grey) has not been crystalized
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