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Nucleic Acids Research, 1990, Vol. 18, No. 9 2801-2806
© 1990

ENZYMOLOGY

Archaebacterial reverse gyrase cleavage-site specificity is similar to that of eubacterial DNA topoisomerases I

O.I. Kovalsky1, S.A. Koyyavkin2 and A.I. Slesarev*

Institute of Molecular Genetics, USSR Academy of Sciences 46 Kurchatov Square, Moscow 123182 1N.D.Zelinsky Institute of Organic Chemistry, USSR Academy of Sciences 47 Leninsky Pr., Moscow 117913 2R.E.Kavetsky Institute for Oncology Problems, Ukrainian SSR Academy of Sciences 45 Vasilkovskaya Street, Kiev 252127, USSR

*To whom correspondence should be addressed

Received September 7, 1989. Accepted February 19, 1990.

ATP-dependent type I topoisomerases from extremely thermophllic archaebacterla - reverse gyrases - drive positive supercoiling of DNA. We showed that reverse gyrase from Desulfurococcus amylolytlcus breaks the DNA at specific sites and covalentty binds to the 5' end. In 30 out of 31 sites located in pBR322 DNA fragments, cleavage occurs at the sequence 5'–CNNN|–(N is any base). The same rule was previously shown to hold for single-stranded DNA breakage by eubacterial topoisomerases I. The relative cleavage frequencies at different sites depend on Mg2+ and temperature. We discuss the possible physiological and mechanistic role of the above specificity of the bacterial topoisomerases I.


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