Nucleic Acid Chaperone Activity of HIV‐1 Nucleocapsid Protein: Critical Role in Reverse Transcription and Molecular Mechanism

Published on Jan 1, 2005in Progress in Nucleic Acid Research and Molecular Biology
· DOI :10.1016/S0079-6603(05)80006-6
Judith G. Levin37
Estimated H-index: 37
(NIH: National Institutes of Health),
Jianhui Guo12
Estimated H-index: 12
(NIH: National Institutes of Health)
+ 1 AuthorsKarin Musier-Forsyth46
Estimated H-index: 46
(UMN: University of Minnesota)
Publisher Summary This chapter focuses on recent biochemical and biophysical studies that examine the nucleic acid chaperone function of HIV‐1 nucleocapsid protein (NC) and its critical role in facilitating specific and efficient reverse transcription. This chapter also describes the effect of NC on individual steps in viral DNA synthesis. This chapter also summarizes what is known about NC structure, NC nucleic acid binding properties, and the contribution of the zinc fingers to chaperone activity. In addition, this chapter also discusses new evidence that provides a model to explain the mechanism of NC's nucleic acid chaperone activity at the molecular level. Characterization of the mechanism of NC's chaperone activity in molecular terms has been invaluable for understanding NC's effect on specific steps in reverse transcription. NC binds nucleic acids noncooperatively and does not rely on protein– protein interactions to drive aggregation and annealing. Instead, NC‐induced nucleic acid aggregation appears to be facilitated by simple polyelectrolyte attraction, similar to that observed for many multivalent cations.
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