AN RNA-BINDING PEPTIDE FROM BOVINE IMMUNODEFICIENCY VIRUS TAT PROTEIN RECOGNIZES AN UNUSUAL RNA STRUCTURE
AN RNA-BINDING PEPTIDE FROM BOVINE IMMUNODEFICIENCY VIRUS TAT PROTEIN RECOGNIZES AN UNUSUAL RNA STRUCTURE
复制标题
DOI：
10.1021/bi00175a046
复制
发表时间：
1994-03-08
期刊：
影响因子：
2.9
通讯作者：
FRANKEL, AD
中科院分区：
文献类型：
--
作者：
CHEN, L;FRANKEL, AD
人类免疫缺陷病毒 (HIV) Tat 蛋白与位于其 mRNA 5' 端的 RNA 发夹 TAR 特异性结合。 Tat 使用碱性氨基酸短区域内的单个精氨酸残基来识别 TAR 中的凸起区域，这里我们表明，来自牛免疫缺陷病毒 (BIV) Tat 蛋白的 17 个氨基酸富含精氨酸的肽也与其 mRNA (BIV TAR) 5' 端的 RNA 发夹结合，但识别 RNA 的不同结构特征，诱变、RNase 图谱和化学干扰实验表明凸起和茎BIV TAR 区域同时被 BIV 肽识别，并且 RNA 采用不寻常的结构。 BIV Tat 以高亲和力和特异性与其 TAR 位点结合，并且与 HIV Tat 不同，BIV Tat 似乎不使用细胞蛋白来稳定体内 RNA 结合。因此，两种相关的病毒激活剂已经进化出相当不同的方式来识别它们的RNA靶标。
The human immunodeficiency virus (HIV) Tat protein binds specifically to an RNA hairpin, TAR, located at the 5' end of its mRNA. Tat uses a single arginine residue within a short region of basic amino acids to recognize a bulge region in TAR, Here we show that a 17 amino acid arginine-rich peptide from the bovine immunodeficiency virus (BIV) Tat protein also binds to an RNA hairpin at the 5' end of its mRNA (BIV TAR), but recognizes different structural features of the RNA, Mutagenesis, RNase mapping, and chemical interference experiments indicate that bulge and stem regions of BIV TAR are recognized simultaneously by the BIV peptide and that the RNA adopts an unusual structure. BIV Tat binds to its TAR site with high affinity and specificity and, unlike HIV Tat, does not appear to use cellular proteins to stabilize RNA binding in vivo. Thus, two related viral activators have evolved rather distinct ways to recognize their RNA targets.