Journal
SCIENCE
Volume 322, Issue 5904, Pages 1092-1097Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1163108
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Funding
- NIH [GM 068518]
- Intramural Research Program of the Center for Cancer Research
- National Cancer Institute
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The reverse transcriptase ( RT) of human immunodeficiency virus ( HIV) catalyzes a series of reactions to convert single- stranded viral RNA into double- stranded DNA for host cell integration. This process requires a variety of enzymatic activities, including DNA polymerization, RNA cleavage, strand transfer, and strand displacement synthesis. We used single- molecule fluorescence resonance energy transfer to probe the interactions between RT and nucleic acid substrates in real time. RT was observed to slide on nucleic acid duplexes, rapidly shuttling between opposite termini of the duplex. Upon reaching the DNA 3' terminus, RT can spontaneously flip into a polymerization orientation. Sliding kinetics were regulated by cognate nucleotides and anti- HIV drugs, which stabilized and destabilized the polymerization mode, respectively. These long- range translocation activities facilitate multiple stages of the reverse transcription pathway, including normal DNA polymerization and strand displacement synthesis.
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