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The basic loop of the RNase H domain of MLV RT is important both for RNase H and for polymerase activity

  1. Author:
    Boyer, P. L.
    Gao, H. Q.
    Frank, P.
    Clark, P. K.
    Hughes, S. H.

  2. Author Address

    NCI Frederick, HIV Drug Resistance Program, POB B, Frederick, MD 21702 USA. NCI Frederick, HIV Drug Resistance Program, Frederick, MD 21702 USA. NCI Frederick, SAIC Frederick, Frederick, MD 21702 USA. Hughes SH NCI Frederick, HIV Drug Resistance Program, POB B, Frederick, MD 21702 USA.
    1. Year: 2001
  2. Journal: Virology
    1. 282
    2. 1
    3. Pages: 206-213
  4. Type of Article: Article
  1. Abstract:

    Escherichia coil RNase H has a basic extension that is involved in binding nucleic acid substrates. This basic extension is present in the RNase H of Moloney murine leukemia virus reverse transcriptase (MLV RT), but has been deleted from the RNase H of HIV-1 RT. Previous work showed that removing the basic loop from MLV RT (the mutant is called DeltaC) blocked viral replication; however, DeltaC MLV RT retained RNase H activity in an in situ gel assay. We prepared recombinant DeltaC MLV RT and compared its activity to wild-type MLV RT The DeltaC mutant is impaired in both polymerase and RNase H activity; the pattern of defects suggests that the basic loop is involved in the binding of MLV RT to a heteropolymeric template-primer.

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