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• W2890854972 startingPage "5137" @default.
• W2890854972 abstract "The initiation of reverse transcription in human immunodeficiency virus-1 is a key early step in the virus replication cycle. During this process, the viral enzyme reverse transcriptase (RT) copies the single-stranded viral RNA (vRNA) genome into double-stranded DNA using human tRNALys3 as a primer for initiation. The tRNA primer and vRNA genome contain several complementary sequences that are important for regulating reverse transcription initiation kinetics. Using single-molecule Förster resonance energy transfer spectroscopy, we demonstrate that the vRNA-tRNA initiation complex is conformationally heterogeneous and dynamic in the absence of RT. As shown previously, nucleic acid-RT interaction is characterized by rapid dissociation constants. We show that extension of the vRNA-tRNA primer binding site helix from 18 base pairs to 22 base pairs stabilizes RT binding to the complex and that the tRNA 5' end has a role in modulating RT binding. RT occupancy on the complex stabilizes helix 1 formation and reduces global structural heterogeneity. The stabilization of helix 1 upon RT binding may serve to destabilize helix 2, the first pause site for RT during initiation, during later steps of reverse transcription initiation." @default.
• W2890854972 created "2018-09-27" @default.
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• W2890854972 date "2018-12-01" @default.
• W2890854972 modified "2023-10-17" @default.
• W2890854972 title "Dynamic Interplay of RNA and Protein in the Human Immunodeficiency Virus-1 Reverse Transcription Initiation Complex" @default.
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• W2890854972 doi "https://doi.org/10.1016/j.jmb.2018.08.029" @default.
• W2890854972 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6289658" @default.
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• W2890854972 hasPublicationYear "2018" @default.
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