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Papers In Press, published online ahead of print December 3, 2001
J. Biol. Chem, 10.1074/jbc.M110131200
Submitted on October 22, 2001
Revised on December 3, 2001
Accepted on December 2, 2001

The domain organization and properties of individual domains of DNA topoisomerase V, a type 1B topoisomerase with DNA repair activities

Galina I. Belova, Rajendra Prasad, Igor V. Nazimov, Samuel H. Wilson, and Alexei I. Slesarev

Fidelity Systems, Inc., Gaithersburg, MD 20879

Corresponding Author: alex{at}fidelitysystems.com

Topoisomerase V (Topo V) is a type IB (eukaryotic-like) DNA topoisomerase. It was discovered in the hyperthermophilic prokaryote Methanopyrus kandleri and is the only topoisomerase with associated apurinic/apyrimidinic (AP) site-processing activities. The structure of Topo V in the free and DNA-bound states was probed by limited proteolysis at 37ºC and 80ºC. The Topo V protein is comprised of (i) a 44 kDa NH2-terminal core subdomain, which contains the active site tyrosine residue, for topoisomerase activity, (ii) an immediately adjacent 16 kDa subdomain that contains degenerate helix-hairpin-helix (HhH) motifs, (iii) a protease sensitive 18 kDa HhH "hinge" region, and (iv) a 34 kDa COOH-terminal HhH domain. Three truncated Topo V polypeptides comprising the NH2-terminal 44 kDa and 16 kDa domains (Topo61), the 44, 16 and 18 kDa domains (Topo78), and the COOH-terminal 34 kDa domain (Topo34) were cloned, purified, and characterized. Both Topo61 and Topo78 are active topoisomerases but in contrast to Topo V these enzymes are inhibited by high salt concentrations. Topo34 has strong DNA-binding ability but shows no topoisomerase activity. Finally, we demonstrate that Topo78 and Topo34 possess AP lyase activities that are important in base excision DNA repair. Thus, Topo V has at least two active sites capable of processing AP DNA. The significance of multiple HhH motifs for Topo V's processivity is discussed.


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