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Journal of Biochemistry Advance Access published online on February 22, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn026
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© 2008 The Japanese Biochemical Society

Inhibition of DNA helicase, ATPase and DNA binding activities of E. coli RecQ helicase by chemotherapeutic agents

Bo Zhang, Ai-hua Zhang, Lei Chen{ddagger} and Xu Guang{ddagger},¶,*

CNRS, UMR 2027, Institut Curie - Section de Recherche, Centre Universitaire, Bâtiment 110, F-91405 Orsay, France.
{ddagger}Sino-French Research Center for Life Sciences and Genomics Rui Jin Hospital, School of Medicine, Jiao Tong University 197 Rui Jin Er Road, Shanghai, 200025, China

*To whom correspondence should be addressed: Dr. Xu Guang Xi: CNRS, UMR 2027, Institut Curie - Section de Recherche, Centre Universitaire, Bâtiment 110, F-91405 Orsay, France. Tel: 33-1-69-86-31-81, Fax: 33-1-69-86-94-29, E-mail: xu-guang.xi{at}curie.u-psud.fr

Received November 27, 2007; Accepted February 17, 2008


  Abstract

RecQ helicases play an essential role in maintaining genetic integrity in all organisms from E. coli to humans. Defects to these enzymes are responsible for three distinct human diseases: Werner syndrome, Bloom syndrome and Rothmund-Thomson syndrome. All three diseases are characterized by a predisposition to cancer due to increased genomic instability. Previous studies on the effects of non-covalent DNA modifications on the catalytic activity of purified Werner and Bloom DNA helicases have shown that both enzymes have similar sensitivity profiles to these DNA binding agents and are most strongly inhibited by the minor groove binder distamycin A. In this study, we show that the sensitivity profiles of E. coli RecQ to a number of DNA binding ligands are different to those observed for WRN and Bloom helicases. These observations may give insights into the differences in molecular mechanisms underlying efficient motor function of RecQ helicases.

Key Words: Helicase, human diseases, DNA modification, minor groove binder, molecular motor


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