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Proceedings Paper

Effect of the HIV-1 nucleocapsid protein on reverse transcriptase pause sites revealed by single molecule microscopy
Author(s): A. Jouonang; F. Przybilla; J. Godet; K. K. Sharma; T. Restlé; H. de Rocquigny; J.-L. Darlix; C. Kenfack; P. Didier; Y. Mély
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Paper Abstract

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.

Paper Details

Date Published: 22 February 2013
PDF: 11 pages
Proc. SPIE 8590, Single Molecule Spectroscopy and Superresolution Imaging VI, 859009 (22 February 2013); doi: 10.1117/12.2003478
Show Author Affiliations
A. Jouonang, Biophotonics and Pharmacology Lab., CNRS (France)
Univ. de Douala (Cameroon)
F. Przybilla, Biophotonics and Pharmacology Lab., CNRS (France)
J. Godet, Biophotonics and Pharmacology Lab., CNRS (France)
K. K. Sharma, Biophotonics and Pharmacology Lab., CNRS (France)
T. Restlé, Üniv. zu Lübeck (Germany)
H. de Rocquigny, Biophotonics and Pharmacology Lab., CNRS (France)
J.-L. Darlix, Biophotonics and Pharmacology Lab., CNRS (France)
C. Kenfack, Biophotonics and Pharmacology Lab., CNRS (France)
Univ. de Douala (Cameroon)
P. Didier, Biophotonics and Pharmacology Lab., CNRS (France)
Y. Mély, Biophotonics and Pharmacology Lab., CNRS (France)


Published in SPIE Proceedings Vol. 8590:
Single Molecule Spectroscopy and Superresolution Imaging VI
Jörg Enderlein; Ingo Gregor; Zygmunt Karol Gryczynski; Rainer Erdmann; Felix Koberling, Editor(s)

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