Reverse gyrase is a DNA topoisomerase that is peculiar in many aspects: it has the unique ability to introduce positive supercoils into DNA molecules; it comprises a type IA topoisomerase fused to a helicase-like domain; although it is a type IA topoisomerase, its reaction is ATP-dependent; and it is the only hyperthermophile-specific protein. All these features have made reverse gyrase the subject of biochemical, structural and functional studies, although they have not shed complete light on the evolution, mechanism and function of this distinctive enzyme. In the present article, we review the latest progress on structure–function relationships of reverse gyrase, and discuss old and recent data linking reverse gyrase to DNA stability, protection and repair in hyperthermophilic organisms.
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February 2009
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Conference Article|
January 20 2009
Reverse gyrase and genome stability in hyperthermophilic organisms
Giuseppe Perugino;
Giuseppe Perugino
1Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy
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Anna Valenti;
Anna Valenti
1Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy
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Anna D'Amaro;
Anna D'Amaro
1Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy
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Mosè Rossi;
Mosè Rossi
1Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy
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Maria Ciaramella
Maria Ciaramella
1
1Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy
1To whom correspondence should be addressed (email m.ciaramella@ibp.cnr.it).
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Publisher: Portland Press Ltd
Received:
September 30 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (1): 69–73.
Article history
Received:
September 30 2008
Citation
Giuseppe Perugino, Anna Valenti, Anna D'Amaro, Mosè Rossi, Maria Ciaramella; Reverse gyrase and genome stability in hyperthermophilic organisms. Biochem Soc Trans 1 February 2009; 37 (1): 69–73. doi: https://doi.org/10.1042/BST0370069
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