Abstract
A broadly applicable genetic strategy was developed for investigating RNA-protein interactions and applied to the HIV-1 Ray protein. By rapidly screening thousands of Rev-RNA interactions in Escherichia coli, we isolated Rev suppressor mutations that alleviated the deleterious effect of mutations in RRE stem-loop IIB, the high affinity RNA-binding site for Rev. All of these suppressor mutations map to a single arginine-deficient face of a Rev α-helix, and some alter the binding specificity of the protein, providing genetic evidence for direct contacts between specific Rev amino acids and RNA nucleotides in the RNA complex of Rev. The spatial constraints suggested by these data have enabled us to model the structure of this complex.
| Original language | English |
|---|---|
| Pages (from-to) | 115-125 |
| Number of pages | 11 |
| Journal | Cell |
| Volume | 87 |
| Issue number | 1 |
| DOIs | |
| State | Published - Oct 1 1996 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
Cite this
A structural model for the HIV-1 Rev-RRE complex deduced from altered- specificity Rev variants isolated by a rapid genetic strategy. / Jain, Chaitanya; Belasco, Joel G.
In: Cell, Vol. 87, No. 1, 01.10.1996, p. 115-125.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A structural model for the HIV-1 Rev-RRE complex deduced from altered- specificity Rev variants isolated by a rapid genetic strategy
AU - Jain, Chaitanya
AU - Belasco, Joel G.
PY - 1996/10/1
Y1 - 1996/10/1
N2 - A broadly applicable genetic strategy was developed for investigating RNA-protein interactions and applied to the HIV-1 Ray protein. By rapidly screening thousands of Rev-RNA interactions in Escherichia coli, we isolated Rev suppressor mutations that alleviated the deleterious effect of mutations in RRE stem-loop IIB, the high affinity RNA-binding site for Rev. All of these suppressor mutations map to a single arginine-deficient face of a Rev α-helix, and some alter the binding specificity of the protein, providing genetic evidence for direct contacts between specific Rev amino acids and RNA nucleotides in the RNA complex of Rev. The spatial constraints suggested by these data have enabled us to model the structure of this complex.
AB - A broadly applicable genetic strategy was developed for investigating RNA-protein interactions and applied to the HIV-1 Ray protein. By rapidly screening thousands of Rev-RNA interactions in Escherichia coli, we isolated Rev suppressor mutations that alleviated the deleterious effect of mutations in RRE stem-loop IIB, the high affinity RNA-binding site for Rev. All of these suppressor mutations map to a single arginine-deficient face of a Rev α-helix, and some alter the binding specificity of the protein, providing genetic evidence for direct contacts between specific Rev amino acids and RNA nucleotides in the RNA complex of Rev. The spatial constraints suggested by these data have enabled us to model the structure of this complex.
UR - http://www.scopus.com/inward/record.url?scp=0030272096&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030272096&partnerID=8YFLogxK
U2 - 10.1016/S0092-8674(00)81328-8
DO - 10.1016/S0092-8674(00)81328-8
M3 - Article
C2 - 8858154
AN - SCOPUS:0030272096
VL - 87
SP - 115
EP - 125
JO - Cell
JF - Cell
SN - 0092-8674
IS - 1
ER -