ARGININE-MEDIATED RNA RECOGNITION - THE ARGININE FORK
ARGININE-MEDIATED RNA RECOGNITION - THE ARGININE FORK
复制标题
DOI：
10.1126/science.252.5009.1167
复制
发表时间：
1991-05-24
期刊：
影响因子：
56.9
通讯作者：
FRANKEL, AD
中科院分区：
文献类型：
--
作者：
CALNAN, BJ;TIDOR, B;FRANKEL, AD
含有HIV-1达特蛋白碱性区域的短肽特异性结合TAR RNA中的凸起区域。含有9个组氨酸（R9）的肽也特异性结合TAR，并且含有R9的突变达特蛋白具有完全的反式激活活性。相比之下，含有9个赖氨酸（K9）的肽结合TAR差，相应的蛋白质只给出边际活动。通过从K9突变体开始并用精氨酸取代赖氨酸残基，鉴定出特异性结合和反式激活所需的单个精氨酸。乙基化干扰实验表明，这精氨酸接触两个相邻的磷酸在RNA凸起。模型构建表明，精氨酸的η-氮和ε-氮可以与相邻的磷酸对形成特定的氢键网络，并且这些排列可能发生在RNA环和凸起附近，而不是在双链A型RNA内。因此，精氨酸侧链通常可用于识别特定的RNA结构。
Short peptides that contain the basic region of the HIV-1 Tat protein bind specifically to a bulged region in TAR RNA. A peptide that contained nine arginines (R9) also bound specifically to TAR, and a mutant Tat protein that contained R9 was fully active for transactivation. In contrast, a peptide that contained nine lysines (K9) bound TAR poorly and the corresponding protein gave only marginal activity. By starting with the K9 mutant and replacing lysine residues with arginines, a single arginine was identified that is required for specific binding and transactivation. Ethylation interference experiments suggest that this arginine contacts two adjacent phosphates at the RNA bulge. Model building suggests that the arginine eta-nitrogens and the epsilon-nitrogen can form specific networks of hydrogen bonds with adjacent pairs of phosphates and that these arrangements are likely to occur near RNA loops and bulges and not within double-stranded A-form RNA. Thus, arginine side chains may be commonly used to recognize specific RNA structures.