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Nucleic Acids Research Advance Access published online on December 5, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn994
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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.

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Topoisomerase II: a fitted mechanism for the chromatin landscape

Joaquim Roca*

Institut de Biologia Molecular de Barcelona, CSIC, Baldiri i Reixac 10, 08028 Barcelona, Spain

*To whom correspondence should be addressed. Tel: +34 934 020 117; Fax: +34 934 034 979; Email: joaquim.roca{at}ibmb.csic.es

Received September 30, 2008. Revised November 21, 2008. Accepted November 25, 2008.

The mechanism by which type-2A topoisomerases transport one DNA duplex through a transient double-strand break produced in another exhibits fascinating traits. One of them is the fine coupling between inter-domainal movements and ATP usage; another is their preference to transport DNA in particular directions. These capabilities have been inferred from in vitro studies but we ignore their significance inside the cell, where DNA configurations markedly differ from those of DNA in free solution. The eukaryotic type-2A enzyme, topoisomerase II, is the second most abundant chromatin protein after histones and its biological roles include the decatenation of newly replicated DNA and the relaxation of polymerase-driven supercoils. Yet, topoisomerase II is also implicated in other cellular processes such as chromatin folding and gene expression, in which the topological transformations catalysed by the enzyme are uncertain. Here, some capabilities of topoisomerase II that might be relevant to infer the enzyme performance in the context of chromatin architecture are discussed. Some aspects addressed are the importance of the DNA rejoining step to ensure genome stability, the regulation of the enzyme activity and of its putative structural role, and the selectively of DNA transport in the chromatin milieu.


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