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Journal of Virology, December 2008, p. 12164-12171, Vol. 82, No. 24
0022-538X/08/$08.00+0     doi:10.1128/JVI.01158-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Human T-Cell Lymphotropic Virus Type 1 Nucleocapsid Protein-Induced Structural Changes in Transactivation Response DNA Hairpin Measured by Single-Molecule Fluorescence Resonance Energy Transfer{triangledown}

Qusai Darugar,1 Hannah Kim,1 Robert J. Gorelick,2 and Christy Landes1*

Department of Chemistry, University of Houston, Houston, Texas 77204-5003,1 AIDS and Cancer Virus Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702-12012

Received 3 June 2008/ Accepted 22 September 2008

Time-resolved single-molecule fluorescence spectroscopy was used to study the human T-cell lymphotropic virus type 1 (HTLV-1) nucleocapsid protein (NC) chaperone activity compared to that of the human immunodeficiency virus type 1 (HIV-1) NC protein. HTLV-1 NC contains two zinc fingers, each having a CCHC binding motif similar to HIV-1 NC. HIV-1 NC is required for recognition and packaging of the viral RNA and is also a nucleic acid chaperone protein that facilitates nucleic acid restructuring during reverse transcription. Because of similarities in structures between the two retroviruses, we have used single-molecule fluorescence energy transfer to investigate the chaperoning activity of the HTLV-1 NC protein. The results indicate that the HTLV-1 NC protein induces structural changes by opening the transactivation response (TAR) DNA hairpin to an even greater extent than HIV-1 NC. However, unlike HIV-1 NC, HTLV-1 NC does not chaperone the strand-transfer reaction involving TAR DNA. These results suggest that, despite its effective destabilization capability, HTLV-1 NC is not as effective at overall chaperone function as is its HIV-1 counterpart.

* Corresponding author. Mailing address: Department of Chemistry, University of Houston, 136 Fleming, Houston, TX 77204-5003. Phone: (713) 743-3288. Fax: (713) 743-2709. E-mail: cflandes{at}uh.edu

{triangledown} Published ahead of print on 1 October 2008.

Journal of Virology, December 2008, p. 12164-12171, Vol. 82, No. 24
0022-538X/08/$08.00+0     doi:10.1128/JVI.01158-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Qualley, D. F., Stewart-Maynard, K. M., Wang, F., Mitra, M., Gorelick, R. J., Rouzina, I., Williams, M. C., Musier-Forsyth, K. (2010). C-terminal Domain Modulates the Nucleic Acid Chaperone Activity of Human T-cell Leukemia Virus Type 1 Nucleocapsid Protein via an Electrostatic Mechanism. J. Biol. Chem. 285: 295-307 [Abstract] [Full Text]  


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