The basic loop of the RNase H domain of MLV RT is important both for RNase H and for polymerase activity
The basic loop of the RNase H domain of MLV RT is important both for RNase H and for polymerase activity
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DOI：
10.1006/viro.2000.0827
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发表时间：
2001-03-30
期刊：
影响因子：
3.7
通讯作者：
Hughes, SH
中科院分区：
文献类型：
--
作者：
Boyer, PL;Gao, HQ;Hughes, SH
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.
