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Nucleic Acids Research Advance Access published online on September 27, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn614
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Regulation of the catalytic function of topoisomerase II alpha through association with RNA

Seung-Won Park1,2, Andrew M. Parrott1, David T. Fritz1, Yongkyu Park2, Michael B. Mathews1 and Chee-Gun Lee1,*

1Department of Biochemistry and Molecular Biology and 2Department of Cell Biology and Molecular Medicine, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, 185 South Orange Avenue, Newark, NJ 07103, USA

*To whom correspondence should be addressed. Tel: +82 973 972 0130; Fax: +82 973 972 5594; Email: leecg{at}umdnj.edu

Received June 17, 2008. Revised September 9, 2008. Accepted September 10, 2008.

Topoisomerase II{alpha} interacts with numerous nuclear factors, through which it is engaged in diverse nuclear events such as DNA replication, transcription and the formation or maintenance of heterochromatin. We previously reported that topoisomerase II{alpha} interacts with RNA helicase A (RHA), consistent with a recent view that topoisomerases and helicases function together. Intrigued by our observation that the RHA–topoisomerase II{alpha} interaction is sensitive to ribonuclease A, we explored whether the RHA–topoisomerase II{alpha} interaction can be recapitulated in vitro using purified proteins and a synthetic RNA. This work led us to an unexpected finding that an RNA-binding activity is intrinsically associated with topoisomerase II{alpha}. Topoisomerase II{alpha} stably interacted with RNA harboring a 3'-hydroxyl group but not with RNA possessing a 3'-phosphate group. When measured in decatenation and relaxation assays, RNA binding influenced the catalytic function of topoisomerase II{alpha} to regulate DNA topology. We discuss a possible interaction of topoisomerase II{alpha} with the poly(A) tail and G/U-rich 3'-untranslated region (3'-UTR) of mRNA as a key step in transcription termination.

Present address: Seung-Won Park, Department of Microbiology, College of Medicine, the Catholic University of Korea, Seoul, 137-701, Republic of Korea


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