Paziewska Agnieszka, Wyrwicz Lucjan S, Bujnicki Janusz M, Bomsztyk Karol, Ostrowski Jerzy
Department of Gastroenterology, Medical Center for Postgraduate Education, Maria Sklodowska-Curie Memorial Cancer Center and Institute of Oncology, 02-781 Warsaw, Poland.
FEBS Lett. 2004 Nov 5;577(1-2):134-40. doi: 10.1016/j.febslet.2004.08.086.
The heterogeneous nuclear ribonucleoprotein (hnRNP) K homology (KH) domain is an evolutionarily conserved module that binds short ribonucleotide sequences. KH domains most often are present in multiple copies per protein. In vitro studies of hnRNP K and other KH domain bearing proteins have yielded conflicting results regarding the relative contribution of each KH domain to the binding of target RNAs. To assess this RNA-binding we used full-length hnRNP K, its fragments and the yeast ortholog as baits in the yeast three-hybrid system. The results demonstrate that in this heterologous in vivo system, the three KH domains bind RNA synergistically and that a single KH domain, in comparison, binds RNA weakly.
不均一核核糖核蛋白(hnRNP)K同源(KH)结构域是一种在进化上保守的模块,可结合短核糖核苷酸序列。KH结构域通常在每个蛋白质中以多个拷贝存在。关于hnRNP K和其他含有KH结构域的蛋白质的体外研究,就每个KH结构域对靶RNA结合的相对贡献得出了相互矛盾的结果。为了评估这种RNA结合,我们使用全长hnRNP K、其片段和酵母直系同源物作为酵母三杂交系统中的诱饵。结果表明,在这种异源体内系统中,三个KH结构域协同结合RNA,相比之下,单个KH结构域与RNA的结合较弱。