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Article
The EMBO Journal (2001) 20, 3282–3291, doi:10.1093/emboj/20.12.3282
DNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsids
Jason A. King2, Ralf Dubielzig3, Dirk Grimm1 and Jürgen A. Kleinschmidt1
1 Applied Tumour Virology Program, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 242, D-69120 Heidelberg, Germany
2 Present address: MRC Centre for Inflammation Research, Edinburgh University, Edinburgh, UK
3 Present address: Medigene AG, Lochhamer Stras zlige 11, D-82152 Martinsried, Germany

To whom correspondence should be addressed
Jürgen A. Kleinschmidt, j.kleinschmidt@dkfz.de

Received 5 March 2001; Revised 25 April 2001; Accepted 27 April 2001.
Abstract
Helicases not only catalyse the disruption of hydrogen bonding between complementary regions of nucleic acids, but also move along nucleic acid strands in a polar fashion. Here we show that the Rep52 and Rep40 proteins of adeno-associated virus type 2 (AAV-2) are required to translocate capsid-associated, single-stranded DNA genomes into preformed empty AAV-2 capsids, and that the DNA helicase function of Rep52/40 is essential for this process. Furthermore, DNase protection experiments suggest that insertion of AAV-2 genomes proceeds from the 3' end, which correlates with the 3'right arrow5' processivity demonstrated for the Rep52/40 helicase. A model is proposed in which capsid-immobilized helicase complexes act as molecular motors to 'pump' single-stranded DNA across the capsid boundary.
Keywords: AAV, DNA helicase, encapsidation, virus
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