Summary information and primary citation

PDB-id
2ms0; SNAP-derived features in text and JSON formats; DNAproDB
Class
viral protein-RNA
Method
NMR
Summary
Solution NMR structure pf trnapro:mlv-nucleocapsid (1:2) complex
Reference
Miller SB, Yildiz FZ, Lo JA, Wang B, D'Souza VM (2014): "A structure-based mechanism for tRNA and retroviral RNA remodelling during primer annealing." Nature, 515, 591-595. doi: 10.1038/nature13709.
Abstract
To prime reverse transcription, retroviruses require annealing of a transfer RNA molecule to the U5 primer binding site (U5-PBS) region of the viral genome. The residues essential for primer annealing are initially locked in intramolecular interactions; hence, annealing requires the chaperone activity of the retroviral nucleocapsid (NC) protein to facilitate structural rearrangements. Here we show that, unlike classical chaperones, the Moloney murine leukaemia virus NC uses a unique mechanism for remodelling: it specifically targets multiple structured regions in both the U5-PBS and tRNA(Pro) primer that otherwise sequester residues necessary for annealing. This high-specificity and high-affinity binding by NC consequently liberates these sequestered residues-which are exactly complementary-for intermolecular interactions. Furthermore, NC utilizes a step-wise, entropy-driven mechanism to trigger both residue-specific destabilization and residue-specific release. Our structures of NC bound to U5-PBS and tRNA(Pro) reveal the structure-based mechanism for retroviral primer annealing and provide insights as to how ATP-independent chaperones can target specific RNAs amidst the cellular milieu of non-target RNAs.

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