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      NMR detection of structures in the HIV-1 5'-leader RNA that regulate genome packaging.

      Science (New York, N.Y.)
      5' Untranslated Regions, Base Pairing, Binding Sites, Codon, Initiator, Dimerization, Genes, gag, Genome, Viral, HIV-1, genetics, physiology, Human Immunodeficiency Virus Proteins, metabolism, Mutagenesis, Site-Directed, Nuclear Magnetic Resonance, Biomolecular, Nucleic Acid Conformation, Nucleocapsid Proteins, Protein Binding, Protein Biosynthesis, RNA, Viral, chemistry, Virus Assembly, gag Gene Products, Human Immunodeficiency Virus

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          Abstract

          The 5'-leader of the HIV-1 genome regulates multiple functions during viral replication via mechanisms that have yet to be established. We developed a nuclear magnetic resonance approach that enabled direct detection of structural elements within the intact leader (712-nucleotide dimer) that are critical for genome packaging. Residues spanning the gag start codon (AUG) form a hairpin in the monomeric leader and base pair with residues of the unique-5' region (U5) in the dimer. U5:AUG formation promotes dimerization by displacing and exposing a dimer-promoting hairpin and enhances binding by the nucleocapsid (NC) protein, which is the cognate domain of the viral Gag polyprotein that directs packaging. Our findings support a packaging mechanism in which translation, dimerization, NC binding, and packaging are regulated by a common RNA structural switch.

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