TY - JOUR TI - RNA-directed remodeling of the HIV-1 protein Rev orchestrates assembly of the Rev–Rev response element complex AU - Jayaraman, Bhargavi AU - Crosby, David C AU - Homer, Christina AU - Ribeiro, Isabel AU - Mavor, David AU - Frankel, Alan D A2 - Sundquist, Wesley I VL - 3 PY - 2014 DA - 2014/12/08 SP - e04120 C1 - eLife 2014;3:e04120 DO - 10.7554/eLife.04120 UR - https://doi.org/10.7554/eLife.04120 AB - The HIV-1 protein Rev controls a critical step in viral replication by mediating the nuclear export of unspliced and singly-spliced viral mRNAs. Multiple Rev subunits assemble on the Rev Response Element (RRE), a structured region present in these RNAs, and direct their export through the Crm1 pathway. Rev-RRE assembly occurs via several Rev oligomerization and RNA-binding steps, but how these steps are coordinated to form an export–competent complex is unclear. Here, we report the first crystal structure of a Rev dimer-RRE complex, revealing a dramatic rearrangement of the Rev-dimer upon RRE binding through re-packing of its hydrophobic protein–protein interface. Rev-RNA recognition relies on sequence-specific contacts at the well-characterized IIB site and local RNA architecture at the second site. The structure supports a model in which the RRE utilizes the inherent plasticity of Rev subunit interfaces to guide the formation of a functional complex. KW - HIV KW - protein-RNA structure KW - nuclear export JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -