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  • Title: Activity of the isolated HIV RNase H domain and specific inhibition by N-hydroxyimides.
    Author: Hang JQ, Rajendran S, Yang Y, Li Y, In PW, Overton H, Parkes KE, Cammack N, Martin JA, Klumpp K.
    Journal: Biochem Biophys Res Commun; 2004 Apr 30; 317(2):321-9. PubMed ID: 15063760.
    Abstract:
    This report describes a procedure to generate enzymatically active, isolated HIV RNase H domain. In contrast to previously described preparations, the RNA cleavage activity of the untagged RNase H domain was surprisingly similar to that of the full-length HIV-RT protein. Signature cleavages at 18 and 9 nucleotides downstream of a recessed RNA 5'-end were retained with the isolated RNase H domain. Activity was strongly decreased by deletion of 3 amino acids from the C-terminus, consistent with an important structural or functional role of the C-terminal alpha-helix. A prototype N-hydroxyimide (2-hydroxy-4H-isoquinoline-1,3-dione) was found to inhibit the activity of the isolated HIV RNase H domain as well as the RNase H activity of full-length HIV reverse transcriptase. In contrast, the compound did not significantly inhibit the structurally closely related Escherichia coli RNase HI. Specific binding of N-hydroxyimide compounds to the isolated RNase H domain was observed by protein fluorescence quenching.
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