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Nucleic Acids Research, 1994, Vol. 22, No. 20 4103-4110
© 1994

RNA

Formation of a stable complex between the human immunodeficiency virus integrase protein and viral DNA

Comelis Vink, Ramon A.Puras Lutzke and Ronald H.A. Plasterk*

Division of Molecular Biology, the Netherlands Cancer Institute Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands

*To whom correspondence should be addressed

Received July 11, 1994. Revised August 30, 1994. Accepted August 30, 1994.

The integrase (IN) protein of the human immunodeficiency virus (HIV) mediates two distinct reactions: (i) specific removal of two nucleotides from the 3' ends of the viral DNA and (ii) integration of the viral DNA into target DNA. Although IN discriminates between specific (viral) DNA and nonspecific DNA in physical in vitro assays, a sequence-specific DNA-binding domain could not be identified in the protein. A nonspecific DNAbinding domain, however, was found at the C terminus of the protein. We examined the DNA-binding characteristics of HIV-1 IN, and found that a stable complex of IN and viral DNA is formed in the presence of Mn2$. The IN - viral DNA complex is resistant to challenge by an excess of competitor DNA. Stable binding of IN to the viral DNA requires that the protein contains an intact N-terminal domain and active site (in the central region of the protein), in addition to the C-terminal DNAbinding domain.


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