During reverse transcription, the HIV-1 RNA is converted by the reverse transcriptase (RT) into proviral DNA. RT is assisted by the HIV-1 nucleocapsid (NCp7) protein that notably increases the ability of RT to synthesize DNA through pause sites. Using single molecule FRET, we monitored the NCp7 effect on the binding of RT to nucleic acid sequences corresponding to two different pause sites. NCp7 was found to modify the distribution of RT orientations on the oligonucleotides and decrease the residence time of RT on one of the pause sites. These results give direct insight into the NCp7 molecular mechanism in reverse transcription.
|Title of host publication||Proceedings Volume 8590, Single Molecule Spectroscopy and Superresolution Imaging VI|
|Publication status||Published - 22.02.2013|
|Event||Single Molecule Spectroscopy and Superresolution Imaging VI - San Francisco, United States|
Duration: 02.02.2013 → 03.02.2013