期刊
SCIENCE
卷 334, 期 6053, 页码 242-245出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1210460
关键词
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资金
- National Institute of General Medical Sciences (NIGMS) [R01 GM42561, R25 MBRS-IMSD GM55036, MARC U*STAR 2T34 GM008663]
- HHMI
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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