FRAGMENTS OF THE HIV-1 TAT PROTEIN SPECIFICALLY BIND TAR RNA
FRAGMENTS OF THE HIV-1 TAT PROTEIN SPECIFICALLY BIND TAR RNA
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DOI：
10.1126/science.2205002
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发表时间：
1990-09-14
期刊：
影响因子：
56.9
通讯作者：
CROTHERS, DM
中科院分区：
文献类型：
--
作者：
WEEKS, KM;AMPE, C;CROTHERS, DM
蛋白水解法产生的人类免疫缺陷病毒1型(HIV-1)Tat蛋白的羧基末端片段包括一个富含精氨酸和赖氨酸的保守区，与反式激活反应RNA序列(TAR)特异结合。一个跨越基本亚域的化学合成的14个残基的多肽也识别TAR，确定这个亚域是RNA相互作用的中心。TAR RNA形成一个稳定的发夹，包括一个六个残基的环、一个三核苷酸的嘧啶凸起和广泛的双链结构。竞争和干扰实验表明，TAT衍生的片段与双链RNA结合，并在嘧啶凸起和邻近的TAR双链上特异性地相互作用。
Proteolytically produced carboxy-terminal fragments of the human immunodefficiency 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.