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Journal of Virology, October 2008, p. 10129-10142, Vol. 82, No. 20
0022-538X/08/$08.00+0     doi:10.1128/JVI.01169-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Retroviral Nucleocapsid Proteins Display Nonequivalent Levels of Nucleic Acid Chaperone Activity {triangledown}

Kristen M. Stewart-Maynard,1 Margareta Cruceanu,2 Fei Wang,2 My-Nuong Vo,1 Robert J. Gorelick,3 Mark C. Williams,2 Ioulia Rouzina,4* and Karin Musier-Forsyth5*

Department of Chemistry and Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota 55455,1 Department of Physics, Northeastern University, Boston, Massachusetts 02115,2 AIDS Vaccine Program, Basic Research Program, SAIC-Frederick, Incorporated, National Cancer Institute-Frederick, Frederick, Maryland 21702,3 Department of Molecular Biology, Biochemistry and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455,4 Departments of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 432105

Received 4 June 2008/ Accepted 29 July 2008

Human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein (NC) is a nucleic acid chaperone that facilitates the remodeling of nucleic acids during various steps of the viral life cycle. Two main features of NC's chaperone activity are its abilities to aggregate and to destabilize nucleic acids. These functions are associated with NC's highly basic character and with its zinc finger domains, respectively. While the chaperone activity of HIV-1 NC has been extensively studied, less is known about the chaperone activities of other retroviral NCs. In this work, complementary experimental approaches were used to characterize and compare the chaperone activities of NC proteins from four different retroviruses: HIV-1, Moloney murine leukemia virus (MLV), Rous sarcoma virus (RSV), and human T-cell lymphotropic virus type 1 (HTLV-1). The different NCs exhibited significant differences in their overall chaperone activities, as demonstrated by gel shift annealing assays, decreasing in the order HIV-1 ~ RSV > MLV >> HTLV-1. In addition, whereas HIV-1, RSV, and MLV NCs are effective aggregating agents, HTLV-1 NC, which exhibits poor overall chaperone activity, is unable to aggregate nucleic acids. Measurements of equilibrium binding to single- and double-stranded oligonucleotides suggested that all four NC proteins have moderate duplex destabilization capabilities. Single-molecule DNA-stretching studies revealed striking differences in the kinetics of nucleic acid dissociation between the NC proteins, showing excellent correlation between nucleic acid dissociation kinetics and overall chaperone activity.

* Corresponding author. Mailing address for Karin Musier-Forsyth: Department of Chemistry, The Ohio State University, 100 W 18th Ave., Columbus, OH 43210. Phone: (614) 292-2021. Fax: (614) 688-5402. E-mail: musier{at}chemistry.ohio-state.edu. Mailing address for Ioulia Rouzina: Department of Molecular Biology, Biochemistry, and Biophysics, University of Minnesota, Minneapolis, MN 55455. Phone: (612) 624-7468. Fax: (612) 625-2163. E-mail: rouzi002{at}umn.edu

{triangledown} Published ahead of print on 6 August 2008.

Journal of Virology, October 2008, p. 10129-10142, Vol. 82, No. 20
0022-538X/08/$08.00+0     doi:10.1128/JVI.01169-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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