FRAGMENTS OF THE HIV-1 TAT PROTEIN SPECIFICALLY BIND TAR RNA

被引:455
作者
WEEKS, KM
AMPE, C
SCHULTZ, SC
STEITZ, TA
CROTHERS, DM
机构
[1] YALE UNIV,DEPT MOLEC BIOPHYS & BIOCHEM,NEW HAVEN,CT 06520
[2] YALE UNIV,HOWARD HUGHES MED INST,NEW HAVEN,CT 06520
关键词
D O I
10.1126/science.2205002
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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, identifing 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.
引用
收藏
页码:1281 / 1285
页数:5
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