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Science 14 September 1990:
Vol. 249. no. 4974, pp. 1281 - 1285
DOI: 10.1126/science.2205002
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Articles

Science, Vol 249, Issue 4974, 1281-1285
Copyright © 1990 by American Association for the Advancement of Science

articles

Fragments of the HIV-1 Tat protein specifically bind TAR RNA

KM Weeks, C Ampe, SC Schultz, TA Steitz, and DM Crothers

Department of Chemistry, Yale University, New Haven, CT.

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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