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Volume 272, Number 17, Issue of April 25, 1997 pp. 11157-11164
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Mutations within the Primer Grip Region of HIV-1 Reverse Transcriptase Result in Loss of RNase H Function

(Received for publication, November 5, 1996, and in revised form, February 19, 1997)

Chockalingam Palaniappan Dagger , Michele Wisniewski Dagger , Pamela S. Jacques § , Stuart F. J. Le Grice § , Philip J. Fay Dagger and Robert A. Bambara Dagger par

From the Departments of Dagger  Biochemistry and Biophysics and  Medicine and the par  Cancer Center, University of Rochester, Rochester, New York 14642 and the § Center for AIDS Research and Division of Infectious Diseases, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106

Human immunodeficiency virus (HIV) DNA synthesis is accompanied by degradation of genomic RNA by the RNase H of reverse transcriptase (RT). Two different modes of RNase H activity appear necessary for complete RNA removal. In one, occurring during minus strand synthesis, positioning of the RNase H is determined by binding of the polymerase active site to the DNA 3'-end. In the other, used for removal of remaining RNA fragments, positioning of RT for RNase H-directed cleavage is determined by the RNA 5'-ends. We attempted to identify RT amino acids responsible for these modes of positioning. Twelve RT mutants, each with one alanine replacement in residues 224 to 235, known as the primer grip region, were examined for catalytic abilities. Six of the examined primer grip mutants, although distant from the RNase H active site were altered in their ability to cleave RNA. The mutants P226A, F227A, G231A, Y232A, E233A, and H235A failed to perform RNA 5'-end-directed RNase H cleavage in heparin-challenged reactions. The last four mutants also lacked DNA synthesis and DNA 3'-end-directed RNase H cleavage activities in challenged reactions. Since mutants P226A and F227A carried out these latter reactions normally, these two residues specifically influence 5'-RNA-directed RNase H catalysis.


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