ArticleJournal of virology2002
Subtle alterations of the native zinc finger structures have dramatic effects on the nucleic acid chaperone activity of human immunodeficiency virus type 1 nucleocapsid protein.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 98 citations in OpenAlex.
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- Prodrug Strategy Extends the Use of Anti-HIV Sulfanylbenzamides for ApplicationACS pharmacology & translational science · 2024Article
- Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States.Viruses · 2020Review
- Significant Differences in RNA Structure Destabilization by HIV-1 GagDp6 and NCp7 Proteins.Viruses · 2020Article
- Inhibition of HIV Maturation via Selective Unfolding and Cross-Linking of Gag Polyprotein by a Mercaptobenzamide Acetylator.Journal of the American Chemical Society · 2019Article
- Retroviral nucleocapsid proteins and DNA strand transfers.Biochimie open · 2018Review
- Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018Review
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- Molecular Basis of Encapsidation of Hepatitis C Virus Genome.Frontiers in microbiology · 2018Review
- Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp.Biophysical journal · 2017Article
- Preclinical evaluation of a mercaptobenzamide and its prodrug for NCp7-targeted inhibition of human immunodeficiency virus.Antiviral research · 2016Article
- Requirements for nucleocapsid-mediated regulation of reverse transcription during the late steps of HIV-1 assembly.Scientific reports · 2016Article
- Insights into the mechanisms of RNA secondary structure destabilization by the HIV-1 nucleocapsid protein.RNA (New York, N.Y.) · 2016Article
- Dynamics of linker residues modulate the nucleic acid binding properties of the HIV-1 nucleocapsid protein zinc fingers.PloS one · 2014Article
- HIV-1 nucleocapsid proteins as molecular chaperones for tetramolecular antiparallel G-quadruplex formation.Journal of the American Chemical Society · 2013Article
- Zinc finger function of HIV-1 nucleocapsid protein is required for removal of 5'-terminal genomic RNA fragments: a paradigm for RNA removal reactions in HIV-1 reverse transcription.Virus research · 2013Article
- Molecular determinants of HIV-1 NCp7 chaperone activity in maturation of the HIV-1 dimerization initiation site.Nucleic acids research · 2013Article
- A protein ballet around the viral genome orchestrated by HIV-1 reverse transcriptase leads to an architectural switch: from nucleocapsid-condensed RNA to Vpr-bridged DNA.Virus research · 2013Article
- HIV type 1 Gag as a target for antiviral therapy.AIDS research and human retroviruses · 2012Review
- Blocking premature reverse transcription fails to rescue the HIV-1 nucleocapsid-mutant replication defect.Retrovirology · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The nucleocapsid protein (NC) of human immunodeficiency virus type 1 has two zinc fingers, each containing the invariant CCHC zinc-binding motif; however, the surrounding amino acid context is not identical in the two fingers. Recently, we demonstrated that zinc coordination is required when NC unfolds complex secondary structures in RNA and DNA minus- and plus-strand transfer intermediates; this property of NC reflects its nucleic acid chaperone activity. Here we have analyzed the chaperone activities of mutants having substitutions of alternative zinc-coordinating residues, i.e., CCHH or CCCC, for the wild-type CCHC motif. We also investigated the activities of mutants that retain the CCHC motifs but have mutations that exchange or duplicate the zinc fingers (mutants 1-1, 2-1, and 2-2); these changes affect amino acid context. Our results indicate that in general, for optimal activity in an assay that measures stimulation of minus-strand transfer and inhibition of nonspecific self-priming, the CCHC motif in the zinc fingers cannot be replaced by CCHH or CCCC and the amino acid context of the fingers must be conserved. Context changes also reduce the ability of NC to facilitate primer removal in plus-strand transfer. In addition, we found that the first finger is a more crucial determinant of nucleic acid chaperone activity than the second finger. Interestingly, comparison of the in vitro results with earlier in vivo replication data raises the possibility that NC may adopt multiple conformations that are responsible for different NC functions during virus replication.
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