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Access to the article is free, however registration and sign-in are required. To access its target sites, HIV reverse transcriptase (RT) slides and flips on nucleic acid substrates. Although 20 years of crystallographic and biochemical studies have illuminated the molecular details of the chemistry of DNA synthesis, there have been relatively few insights into how RT finds the end of the nucleic acid substrate where it begins DNA synthesis, how it displaces nucleic acid fragments, or where and how it executes masterful leaps when transferring DNA between templates. On page 1092 of this issue, Liu et al. (2) describe elegant single-molecule fluorescence resonance energy transfer (FRET) experiments that provide a view of RT at work. They show that RT has a remarkable ability to slide on nucleic acid duplexes, rapidly shuttling between the two ends and flipping into the polymerase-competent binding mode when needed.

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Resource Type: Journal article/Issue, Review, Diagram
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16

Author and Copyright

Authors and Editors: Stefan G. Sarafianos of Christopher S. Bond Life Sciences Center, University of Missouri, Eddy Arnold of Department of Molecular Microbiology and Immunology, Rutgers University
Publisher: AAAS
Format: text/html
Copyright and other restrictions: Yes
Cost: No


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