NDLI: Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.

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Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Edgcomb, Stephen P. Gerace, Larry Williamson, James R. Hennig, Mirko Kompfner, Elizabeth Aschrafi, Angelique
Description	Country affiliation: United States Author Affiliation: Edgcomb SP ( Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.)
Abstract	The translation of the unspliced and partially spliced viral mRNAs that encode the late, structural proteins of HIV-1 depends on the viral-protein Rev. Oligomeric binding of Rev to the Rev response element (RRE) in these mRNAs promotes their export from the nucleus and thus controls their expression. Here, we compared the effects of hydrophobic to hydrophilic mutations within the oligomerization domain of Rev using assays for oligomeric RNA binding, protein structure, and export from the nucleus. Oligomeric RNA binding alone does not correlate well with RNA transport activity in the subset of mutants. However, protein structure as judged by CD spectroscopy does correlate well with Rev function. The oligomeric assembly of Rev-L18T is impaired but exhibits minor defects in structure and retains a basal level of activity in vivo. The prevalence of L18T in infected individuals suggests a positive selection mechanism for L18T modulation of Rev activity that may delay the onset of AIDS.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1110/ps.073246608
Journal	Protein Science
Issue Number	3
Volume Number	17
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2008-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Rna, Viral Chemistry Rev Gene Products, Human Immunodeficiency Virus Amino Acid Sequence Binding Sites Genes, Reporter Genetic Variation Hela Cells Molecular Sequence Data Mutation Point Mutation Protein Binding Protein Conformation Protein Structure, Tertiary Rna Transport Rna, Messenger Metabolism Sequence Alignment Genetics Research Support, N.i.h., Extramural Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev–RRE complexes

A Long-Awaited Structure Is Rev-ealed

Structural basis for cooperative RNA binding and export complex assembly by HIV Rev

RNA-guided assembly of Rev-RRE nuclear export complexes

Human immunodeficiency virus type 1 regulator of virion expression, rev, forms nucleoprotein filaments after binding to a purine-rich 'bubble' located within the rev-responsive region of viral mRNAs.

Specific RNA Binding by a Single C2H2Zinc Finger

Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB.

Interaction of the HIV-1 rev cofactor eukaryotic initiation factor 5A with ribosomal protein L5.

Enhancement of coenzyme binding by a single point mutation at the coenzyme binding domain of E. coli lactaldehyde dehydrogenase.

Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.

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Protein structure and oligomerization are important for the formation of export-competent HIV-1 Rev-RRE complexes.