Base flexibility in HIV-2 TAR RNA mapped by solution 15N,13C NMR relaxation
Base flexibility in HIV-2 TAR RNA mapped by solution 15N,13C NMR relaxation
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DOI：
10.1006/jmbi.2001.5424
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发表时间：
2002-03-22
影响因子：
5.6
通讯作者：
Williamson, JR
中科院分区：
文献类型：
--
作者：
Dayie, KT;Brodsky, AS;Williamson, JR
HIV蛋白与TAR（反激活反应区）RNA元件结合可激活HIV病毒基因组的转录。TAR与精氨酸酰胺的复合物可作为TAR -TAR复合物中RNA构象的模型。通过测量质子化碱基碳核和氮核的弛豫速率，研究了HIV-2 tar -精氨酸酰胺复合物的动力学。测量了6个自相关率以及相互相关率，以绘制HIV-2 tar -精氨酸酰胺复合物中碱基运动的频率。这些测量揭示了六核苷酸环、二核苷酸凸起和a型螺旋区所表现出的广泛的动态异质性。凸起处的U23在结合精氨酸酰胺时发生的动态变化最大，而U25则保持弹性，反映了配体结合时引发的较大构象变化。(C) 2002 Elsevier Science Ltd.
Binding of the HIV tat protein to the TAR (transactivating response region) RNA element activates transcription of the HIV viral genome. The complex of TAR with argininamide serves as a model for the RNA conformation in the tat-TAR complex. The dynamics of the HIV-2 TAR-argininamide complex was investigated by measurements of the relaxation rates of protonated base carbon and nitrogen nuclei. Six autocorrelation rates as well as cross-correlation rates were measured to map the frequencies of base motion in the HIV-2 TAR-argininamide complex. These measurements reveal a broad range of dynamic heterogeneity exhibited by hexanucleotide loop, the dinucleotide bulge, and the A-form helical regions. U23 in the bulge undergoes the largest dynamic change on binding argininamide, while U25 remains flexible, reflecting the large conformational change that is triggered upon ligand binding. (C) 2002 Elsevier Science Ltd.