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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.

Escherichia coli 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.[1]

References

  1. The basic loop of the RNase H domain of MLV RT is important both for RNase H and for polymerase activity. Boyer, P.L., Gao, H.Q., Frank, P., Clark, P.K., Hughes, S.H. Virology (2001) [Pubmed]
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