ArticleAnalytical biochemistry2006
Single DNA molecule stretching measures the activity of chemicals that target the HIV-1 nucleocapsid protein.
Article in Analytical biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 39 citations in OpenAlex.
- Inhibitory Effect of Lithospermic Acid on the HIV-1 Nucleocapsid Protein.Molecules (Basel, Switzerland) · 2020Article
- Article
- Identification and characterization of a new type of inhibitor against the human immunodeficiency virus type-1 nucleocapsid protein.Retrovirology · 2015Article
- Single aromatic residue location alters nucleic acid binding and chaperone function of FIV nucleocapsid protein.Virus research · 2014Article
- Differential contribution of basic residues to HIV-1 nucleocapsid protein's nucleic acid chaperone function and retroviral replication.Nucleic acids research · 2014Article
- Identification of HIV-1 inhibitors targeting the nucleocapsid protein.Journal of medicinal chemistry · 2012Article
- A single zinc finger optimizes the DNA interactions of the nucleocapsid protein of the yeast retrotransposon Ty3.Nucleic acids research · 2012Article
- Biophysical characterization of DNA binding from single molecule force measurements.Physics of life reviews · 2010Review
- Effects of the nature and concentration of salt on the interaction of the HIV-1 nucleocapsid protein with SL3 RNA.Biochemistry · 2010Article
- Retroviral nucleocapsid proteins display nonequivalent levels of nucleic acid chaperone activity.Journal of virology · 2008Article
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Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
We develop a biophysical method for investigating chemical compounds that target the nucleic acid chaperone activity of HIV-1 nucleocapsid protein (NCp7). We used an optical tweezers instrument to stretch single lambda-DNA molecules through the helix-coil transition in the presence of NCp7 and various chemical compounds. The change in the helix-coil transition width induced by wild-type NCp7 and its zinc finger variants correlates with in vitro nucleic acid chaperone activity measurements and in vivo assays. The compound-NC interaction measured here reduces NCp7's capability to alter the transition width. Purified compounds from the NCI Diversity set, 119889, 119911, and 119913 reduce the chaperone activity of 5 nM NC in aqueous solution at 10, 25, and 100 nM concentrations respectively. Similarly, gallein reduced the activity of 4 nM NC at 100 nM concentration. Further analysis allows us to dissect the impact of each compound on both sequence-specific and non-sequence-specific DNA binding of NC, two of the main components of NC's nucleic acid chaperone activity. These results suggest that DNA stretching experiments can be used to screen chemical compounds targeting NC proteins and to further explore the mechanisms by which these compounds interact with NC and alter its nucleic acid chaperone activity.
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