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Special Issue "DNA Topoisomerase: Structure, Function and Mechanism and Regulation of Activities"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: 31 December 2020.

Special Issue Editor

Prof. Dagmar Klostermeier
Guest Editor
Westfälische Wilhelms-Universität Münster, Muenster, Germany
Interests: topoisomerases; helicases; enzyme mechanism; single-molecule FRET; conformational changes

Special Issue Information

Dear Colleagues,

DNA topoisomerases mediate changes in DNA topology. By relaxing and supercoiling DNA, by resolving or generating catenanes, or by introducing and removing knots, these enzymes resolve topological issues pertaining to DNA recombination, replication, and repair, as well as transcription, and maintain the topological state of DNA in the cell. Topoisomerases are grouped into different families according to common features in their structure and/or the mechanisms of the reaction they catalyze. However, structural and mechanistic insight gained in the past years has shown that there are a number of variations to these common themes, enabling the optimization of each enzyme for its physiological task, and allowing for species-specific variations and fine-tuning of activities. Genome-wide studies have defined the sites of topoisomerase binding to and action on DNA under physiological conditions, providing insights into cellular function and the regulation of their activities.

This Special Issue focuses on the structure, function, and mechanism of DNA topoisomerases and the regulation of their activities. Research articles report novel insights into specific aspects of DNA topoisomerases, while review articles highlight recent advances and summarize the current status of the field.

Prof. Dagmar Klostermeier
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • Topoisomerase structure
  • Topoisomerase mechanism
  • Regulation of topoisomerase activity
  • Supercoiling
  • Relaxation
  • Decatenation

Published Papers (1 paper)

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Open AccessReview
Mechanism of Type IA Topoisomerases
Molecules 2020, 25(20), 4769; - 17 Oct 2020
Topoisomerases in the type IA subfamily can catalyze change in topology for both DNA and RNA substrates. A type IA topoisomerase may have been present in a last universal common ancestor (LUCA) with an RNA genome. Type IA topoisomerases have since evolved to [...] Read more.
Topoisomerases in the type IA subfamily can catalyze change in topology for both DNA and RNA substrates. A type IA topoisomerase may have been present in a last universal common ancestor (LUCA) with an RNA genome. Type IA topoisomerases have since evolved to catalyze the resolution of topological barriers encountered by genomes that require the passing of nucleic acid strand(s) through a break on a single DNA or RNA strand. Here, based on available structural and biochemical data, we discuss how a type IA topoisomerase may recognize and bind single-stranded DNA or RNA to initiate its required catalytic function. Active site residues assist in the nucleophilic attack of a phosphodiester bond between two nucleotides to form a covalent intermediate with a 5′-phosphotyrosine linkage to the cleaved nucleic acid. A divalent ion interaction helps to position the 3′-hydroxyl group at the precise location required for the cleaved phosphodiester bond to be rejoined following the passage of another nucleic acid strand through the break. In addition to type IA topoisomerase structures observed by X-ray crystallography, we now have evidence from biophysical studies for the dynamic conformations that are required for type IA topoisomerases to catalyze the change in the topology of the nucleic acid substrates. Full article
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