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Journal of Virology, November 2001, p. 10132-10138, Vol. 75, No. 21
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.21.10132-10138.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Requirements for Minus-Strand Transfer Catalyzed by Rous Sarcoma Virus Reverse Transcriptase

Susanne Werner, Karin Vogel-Bachmayr, Britta Hollinderbäumer, and Birgitta M. Wöhrl*

Abteilung Physikalische Biochemie, Max-Planck-Institut für Molekulare Physiologie, 44227 Dortmund, Germany

Received 19 March 2001/Accepted 2 August 2001

We have examined the specific minus-strand transfer reactions that occur after the synthesis of minus strong-stop DNA and nonspecific strand switching on homopolymeric poly(rA) templates with different types of Rous sarcoma virus (RSV) reverse transcriptases. Three different types of reverse transcriptases can be isolated from virions of RSV: heterodimeric alpha beta and homodimeric alpha  and beta . The mechanism of minus-strand transfer was examined using a model primer-template substrate corresponding to the 5'- and 3'-terminal RNA regions of the RSV genome. The results reveal that the RNase H activity of RSV reverse transcriptases is required for minus-strand transfer. Less than 2% of strand transfer of the extended product is detectable with RNase H-deficient enzymes. We could show that the alpha  homodimer lacking the integrase domain can perform strand transfer almost as efficiently as the alpha beta and alpha Pol heterodimers. In contrast, the activities of beta  and Pol for minus-strand transfer are reduced. Furthermore, a two- to fivefold increase in minus-strand transfer activities was observed in the presence of human immunodeficiency virus type 1 nucleocapsid protein.

* 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, November 2001, p. 10132-10138, Vol. 75, No. 21
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.21.10132-10138.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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  • Guo, J., Wu, T., Kane, B. F., Johnson, D. G., Henderson, L. E., Gorelick, R. J., Levin, J. G. (2002). Subtle Alterations of the Native Zinc Finger Structures Have Dramatic Effects on the Nucleic Acid Chaperone Activity of Human Immunodeficiency Virus Type 1 Nucleocapsid Protein. J. Virol. 76: 4370-4378 [Abstract] [Full Text]  


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