Abstract:
:DNA topoisomerase II (topo II) changes DNA topology by cleavage/re-ligation cycle(s) and thus contributes to various nuclear DNA transactions. It is largely unknown how the enzyme is controlled in a nuclear context. Several studies have suggested that its C-terminal domain (CTD), which is dispensable for basal relaxation activity, has some regulatory influence. In this work, we examined the impact of nuclear localization on regulation of activity in nuclei. Specifically, human cells were transfected with wild-type and mutant topo IIβ tagged with EGFP. Activity attenuation experiments and nuclear localization data reveal that the endogenous activity of topo IIβ is correlated with its subnuclear distribution. The enzyme shuttles between an active form in the nucleoplasm and a quiescent form in the nucleolus in a dynamic equilibrium. Mechanistically, the process involves a tethering event with RNA. Isolated RNA inhibits the catalytic activity of topo IIβ in vitro through the interaction with a specific 50-residue region of the CTD (termed the CRD). Taken together, these results suggest that both the subnuclear distribution and activity regulation of topo IIβ are mediated by the interplay between cellular RNA and the CRD.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Onoda A,Hosoya O,Sano K,Kiyama K,Kimura H,Kawano S,Furuta R,Miyaji M,Tsutsui K,Tsutsui KMdoi
10.1093/nar/gku640subject
Has Abstractpub_date
2014-08-01 00:00:00pages
9005-20issue
14eissn
0305-1048issn
1362-4962pii
gku640journal_volume
42pub_type
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