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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
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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