Document 2063
 DOCN  M94A2063
 TI    RNase H domain of HIV-2: crystal structure and reconstitution of the
       activity.
 DT    9412
 AU    Hostomska Z; Matthews DA; Knighton DR; Hostomsky Z
 SO    Int Conf AIDS. 1994 Aug 7-12;10(1):39 (abstract no. 128A). Unique
       Identifier : AIDSLINE ICA10/94370512
 AB    The HIV reverse transcriptase (RT) is a multifunctional enzyme which
       displays DNA- and RNA-dependent DNA polymerase and RNase H activities.
       RNase H activity, which resides in 15 kD C-terminal region of p66
       subunit of RT, is required for viral replication. To design compounds
       active against RNase H of both HIV-1 and HIV-2 it is important to
       understand the molecular details of their structures. We characterized
       enzymatic activity of HIV-2 RNase H and compared crystal structures of
       HIV-1 and HIV-2 RNase H. HIV-2 RNase H domain (of ISY strain) is 60%
       identical to that of HIV-1 (strain BH10). They are no insertion or
       deletions. We found that while the RNase H domain exhibit no detectable
       activity when expressed separately, the activity can be reconstituted by
       combining RNase H and DNA polymerase domains. Interestingly, the
       activity of isolated HIV-2 RNase H can be reconstituted not only in the
       presence of the HIV-2 polymerase domain but also with the HIV-1
       polymerase domain. It suggests that sites involved in specific
       interdomain interactions in RT are conserved between HIV-1 and HIV-2.
       The purified HIV-2 RNase H domain was crystallized in a triclinic cell
       and its structure was determined. The structural model of HIV-2 RNase H
       will be presented.
 DE    DNA Polymerases/CHEMISTRY  HIV-1/ENZYMOLOGY  HIV-2/*ENZYMOLOGY
       Molecular Structure  Ribonuclease H, Calf Thymus/*CHEMISTRY/GENETICS
       MEETING ABSTRACT

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