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Open AccessReview

HIV Rev Assembly on the Rev Response Element (RRE): A Structural Perspective

Reverse Transcriptase Biochemistry Section, Basic Research Program, Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA
Author to whom correspondence should be addressed.
Academic Editor: David Boehr
Viruses 2015, 7(6), 3053-3075;
Received: 8 May 2015 / Accepted: 5 June 2015 / Published: 12 June 2015
HIV-1 Rev is an ~13 kD accessory protein expressed during the early stage of virus replication. After translation, Rev enters the nucleus and binds the Rev response element (RRE), a ~350 nucleotide, highly structured element embedded in the env gene in unspliced and singly spliced viral RNA transcripts. Rev-RNA assemblies subsequently recruit Crm1 and other cellular proteins to form larger complexes that are exported from the nucleus. Once in the cytoplasm, the complexes dissociate and unspliced and singly-spliced viral RNAs are packaged into nascent virions or translated into viral structural proteins and enzymes, respectively. Rev binding to the RRE is a complex process, as multiple copies of the protein assemble on the RNA in a coordinated fashion via a series of Rev-Rev and Rev-RNA interactions. Our understanding of the nature of these interactions has been greatly advanced by recent studies using X-ray crystallography, small angle X-ray scattering (SAXS) and single particle electron microscopy as well as biochemical and genetic methodologies. These advances are discussed in detail in this review, along with perspectives on development of antiviral therapies targeting the HIV-1 RRE. View Full-Text
Keywords: HIV; Rev; Rev response element; RRE; Crm1; nuclear export complex HIV; Rev; Rev response element; RRE; Crm1; nuclear export complex
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MDPI and ACS Style

Rausch, J.W.; Grice, S.F.J.L. HIV Rev Assembly on the Rev Response Element (RRE): A Structural Perspective. Viruses 2015, 7, 3053-3075.

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