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J. Biol. Chem., Vol. 276, Issue 33, 31429-31438, August 17, 2001
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From the Unité de Physicochimie des Macromolécules
Biologiques, Institut Pasteur, URA1773 du CNRS,
75724 Paris Cedex 15, France
Human immunodeficiency virus, type 1 (HIV-1)
reverse transcriptase (RT) terminates plus-strand DNA synthesis at the
center of the HIV-1 genome, a process important for HIV-1 infectivity. The central termination sequence contains two termination sites (Ter1 and Ter2) located at the 3'-end of AnTm motifs,
and the narrowing of the DNA minor groove generated by these motifs is
responsible for termination. Kinetic data associated with the
binding of RT and its ability to elongate in vitro various DNA duplexes and triplexes surrounding the Ter2 terminator were analyzed using a simple kinetic scheme. At Ter2, RT still displays a
reasonable affinity for the corresponding DNA, but the binding of the
next nucleotide and above all its incorporation rate are markedly
hampered. Features affecting the width of the minor groove act directly
at this last step. The constraint exerted against elongation by the
AnTm tract persists at two positions downstream of the terminator.
To whom correspondence should be addressed: Dept. of Molecular
Biology, Wellman 10, Massachusetts General Hospital, Fruit St., Boston,
MA 02114. E-mail: lavigne@molbio.mgh.harvard.edu.
§
Present address: Dept. of Molecular Biology, Institut Pasteur,
75724 Paris Cedex 15, France.
¶
Present address: URA 1960 CNRS, Institut Pasteur, 75724 Paris
Cedex 15, France.
This article has been cited by other articles:
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M. Lavigne, L. Polomack, and H. Buc Structures of Complexes Formed by HIV-1 Reverse Transcriptase at a Termination Site of DNA Synthesis J. Biol. Chem., August 10, 2001; 276(33): 31439 - 31448. [Abstract] [Full Text] [PDF] |
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