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Journal of Virology, June 2002, p. 6205-6212, Vol. 76, No. 12
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.12.6205-6212.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Subcellular Localization and Integration Activities of Rous Sarcoma Virus Reverse Transcriptase

Susanne Werner,1 Patrick Hindmarsh,2 Markus Napirei,3 Karin Vogel-Bachmayr,1 and Birgitta M. Wöhrl1*

Max-Planck-Institut für Molekulare Physiologie, Abteilung Physikalische Biochemie, 44227 Dortmund,1 Ruhr-Universität Bochum, Medizinische Fakultät, Abteilung für Anatomie und Embryologie, 44801 Bochum, Germany,3 Department of Microbiology and Immunology, Northwestern University School of Medicine, Chicago, Illinois 606112

Received 18 July 2001/ Accepted 12 March 2002

Reverse transcriptases (RTs) {alpha}ß and ß from avian Rous sarcoma virus (RSV) harbor an integrase domain which is absent in nonavian retroviral RTs. RSV integrase contains a nuclear localization signal which enables the enzyme to enter the nucleus of the cell in order to perform integration of the proviral DNA into the host genome. In the present study we analyzed the subcellular localization of RSV RT, since previous results indicated that RSV finishes synthesis of the proviral DNA in the nucleus. Our results demonstrate that the heterodimeric RSV RT {alpha}ß and the ß subunit, when expressed independently, can be detected in the nucleus, whereas the separate {alpha} subunit lacking the integrase domain is prevalent in the cytoplasm. These data suggest an involvement of RSV RT in the transport of the preintegration complex into the nucleus. In addition, to analyze whether the integrase domain, located at the carboxyl terminus of ß, exhibits integration activities, we investigated the nicking and joining activities of heterodimeric RSV RT {alpha}ß with an oligodeoxynucleotide-based assay system and with a donor substrate containing the supF gene flanked by the viral long terminal repeats. Our data show that RSV RT {alpha}ß is able to perform the integration reaction in vitro; however, it does so with an estimated 30-fold lower efficiency than the free RSV integrase, indicating that RSV RT is not involved in integration in vivo. Integration with RSV RT {alpha}ß could be stimulated in the presence of human immunodeficiency virus type 1 nucleocapsid protein or HMG-I(Y).

* Corresponding author. Mailing address: Max-Planck-Institut für Molekulare Physiologie, Abteilung Physikalische Biochemie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany. Phone: 49-231-133-2312. Fax: 49-231-133-2399. E-mail: birgit.woehrl{at}mpi-dortmund.mpg.de.

Journal of Virology, June 2002, p. 6205-6212, Vol. 76, No. 12
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.12.6205-6212.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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