Abstract
Proteolytically produced carboxyl-terminal fragments of the human immunodeficiency virus type-1 (HIV-1) Tat protein that include a conserved region rich in arginine and lysine bind specifically to transactivation response RNA sequences (TAR). A chemically synthesized 14-residue peptide spanning the basic subdomain also recognizes TAR, identifying this subdomain as central for RNA interaction. TAR RNA forms a stable hairpin that includes a six-residue loop, a trinucleotide pyrimidine bulge, and extensive duplex structure. Competition and interference experiments show that the Tat-derived fragments bind to double-stranded RNA and interact specifically at the pyrimidine bulge and adjacent duplex of TAR.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 6:10 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 5:19 a.m.) |
Indexed | 1 month, 3 weeks ago (July 4, 2025, 7:26 a.m.) |
Issued | 34 years, 11 months ago (Sept. 14, 1990) |
Published | 34 years, 11 months ago (Sept. 14, 1990) |
Published Print | 34 years, 11 months ago (Sept. 14, 1990) |
@article{Weeks_1990, title={Fragments of the HIV-1 Tat Protein Specifically Biand TAR RNA}, volume={249}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2205002}, DOI={10.1126/science.2205002}, number={4974}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Weeks, Kevin M. and Ampe, Christophe and Schultz, Steve C. and Steitz, Thomas A. and Crothers, Donald M.}, year={1990}, month=sep, pages={1281–1285} }