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J. Biol. Chem., Vol. 278, Issue 33, 30755-30763, August 15, 2003

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Differing Roles of the N- and C-terminal Zinc Fingers in Human Immunodeficiency Virus Nucleocapsid Protein-enhanced Nucleic Acid Annealing^*

Megan J. Heath , Suchitra S. Derebail , Robert J. Gorelick  and Jeffrey J. DeStefano  ¶

From the Department of Cell Biology and Molecular Genetics, University of Maryland College Park, College Park, Maryland 20742 and the AIDS Vaccine Program, SAIC-Frederick, Inc., NCI-Frederick, Frederick, Maryland 21702

The replication process of human immunodeficiency virus requires a number of nucleic acid annealing steps facilitated by the hybridization and helix-destabilizing activities of human immunodeficiency virus nucleocapsid (NC) protein. NC contains two CCHC zinc finger motifs numbered 1 and 2 from the N terminus. The amino acids surrounding the CCHC residues differ between the two zinc fingers. Assays were preformed to investigate the activities of the fingers by determining the effect of mutant and wild-type proteins on annealing of 42-nucleotide RNA and DNA complements. The mutants 1.1 NC and 2.2 NC had duplications of the N- and C-terminal zinc fingers in positions 1 and 2. The mutant 2.1 NC had the native zinc fingers with their positions switched. Annealing assays were completed with unstructured and highly structured oligonucleotide complements. 2.2 NC had a near wild-type level of annealing of unstructured nucleic acids, whereas it was completely unable to stimulate annealing of highly structured nucleic acids. In contrast, 1.1 NC was able to stimulate annealing of both unstructured and structured substrates, but to a lesser degree than the wild-type protein. Results suggest that finger 1 has a greater role in unfolding of strong secondary structures, whereas finger 2 serves an accessory role that leads to a further increase in the rate of annealing.

Received for publication, April 11, 2003 , and in revised form, June 2, 2003.

^* This work was supported by National Institutes of Health Grant GM51140 and by NCI Contract N01-CO-12400 from the National Institutes of Health with SAIC-Frederick, Inc. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Dept. of Cell Biology and Molecular Genetics, University of Maryland, Bldg. 231, College Park, MD 20742. Tel.: 301-405-5449; Fax: 301-314-9489; E-mail: jd146{at}umail.umd.edu.

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