NDLI: Mutations in the RNase H domain of HIV-1 reverse transcriptaseaffect the initiation of DNA synthesis and the specificity of RNase Hcleavage in vivo

Content Provider	PubMed Central
Author	Julias, John G. Mcwilliams, Mary Jane Sarafianos, Stefan G. Arnold, Edward Hughes, Stephen H.
Copyright Year	2002
Abstract	Retroviral reverse transcriptases contain a DNA polymerase activitythat can copy an RNA or DNA template and an RNase H activity thatdegrades the viral RNA genome during reverse transcription. RNase Hmakes both specific and nonspecific cleavages; specific cleavages areused to generate and remove the polypurine tract primer used forplus-strand DNA synthesis and to remove the tRNA primer used forminus-strand DNA synthesis. We generated mutations in an HIV-1-basedvector to change amino acids in the RNase H domain that contact eitherthe RNA and DNA strands. Some of these mutations affected theinitiation of DNA synthesis, demonstrating an interdependence of thepolymerase and RNase H activities of HIV-1 reverse transcription duringviral DNA synthesis. The ends of the linear DNA form of the HIV-1genome are defined by the specific RNase H cleavages that remove theplus- and minus-strand primers; these ends can be joined to formtwo-long-terminal repeat circles. Analysis of two-long-terminalrepeat circle junctions showed that mutations in the RNase Hdomain affect the specificity of RNase H cleavage.
Related Links	http://dx.doi.org/10.1073/pnas.142123199
Starting Page	9515
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-07-09
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo.

Altered error specificity of RNase H-deficient HIV-1 reverse transcriptases during DNA-dependent DNA synthesis

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