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The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly

DOI: 10.1016/j.str.2016.04.015 DOI Help

Authors: Mike Dimattia (National Institute of Arthritis and Musculoskeletal and Skin Diseases, University of Oxford) , Norman r. Watts (National Institute of Arthritis and Musculoskeletal and Skin Diseases) , Naiqian Cheng (National Institute of Arthritis and Musculoskeletal and Skin Diseases) , Rick Huang (National Institute of Arthritis and Musculoskeletal and Skin Diseases) , J. bernard Heymann (National Institute of Arthritis and Musculoskeletal and Skin Diseases) , Jonathan Grimes (Division of Structural Biology, University of Oxford, Diamond Light Source) , Paul t. Wingfield (National Institute of Arthritis and Musculoskeletal and Skin Diseases) , David i. Stuart (University of Oxford, Diamond Light Source) , Alasdair c. Steven (National Institute of Arthritis and Musculoskeletal and Skin Diseases)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure , VOL 24 , PAGES 1068 - 1080

State: Published (Approved)
Published: July 2016

Abstract: HIV-1 Rev protein mediates the nuclear export of viral RNA genomes. To do so, Rev oligomerizes cooperatively onto an RNA motif, the Rev response element (RRE), forming a complex that engages with the host nuclear export machinery. To better understand Rev oligomerization, we determined four crystal structures of Rev N-terminal domain dimers, which show that they can pivot about their dyad axis, giving crossing angles of 90° to 140°. In parallel, we performed cryoelectron microscopy of helical Rev filaments. Filaments vary from 11 to 15nm in width, reflecting variations in dimer crossing angle. These structures contain additional density, indicating that C-terminal domains become partially ordered in the context of filaments. This conformational variability may be exploited in the assembly of RRE/Rev complexes. Our data also revealed a third interface between Revs, which offers an explanation for how the arrangement of Rev subunits adapts to the "A"-shaped architecture of the RRE in export-active complexes.

Subject Areas: Biology and Bio-materials, Medicine, Chemistry


Instruments: I02-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: European Synchrotron Radiation Facility (Grenoble, France) beamline ED23-EH2

Added On: 15/08/2016 10:50

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