Luz N, Beck E
Zentrum für Molekulare Biologie Heidelberg, University of Heidelberg, Germany.
J Virol. 1991 Dec;65(12):6486-94. doi: 10.1128/JVI.65.12.6486-6494.1991.
A cellular 57-kDa protein (p57) that binds specifically to the internal translation initiation site in the 5' untranslated region of foot-and-mouth disease virus RNA was detected in cell extracts of different mammalian species by UV cross-linking. The protein binds to two distinct sites of the translation control region which have as the only common sequence a UUUC motif. The first binding site consists of a conserved hairpin structure, whereas the second binding site contains an essential pyrimidine-rich region without obvious secondary structure. Competition experiments indicate that the complexes with the two binding sites were formed by a single p57 species. The protein binds also to the 5' untranslated region of other picornaviruses. Results from footprint analyses with foot-and-mouth disease RNA suggest the participation of additional cellular factors in the translation initiation complex.
通过紫外线交联在不同哺乳动物物种的细胞提取物中检测到一种细胞57 kDa蛋白（p57），它特异性结合口蹄疫病毒RNA 5'非翻译区的内部翻译起始位点。该蛋白与翻译控制区的两个不同位点结合，这两个位点唯一的共同序列是一个UUUC基序。第一个结合位点由一个保守的发夹结构组成，而第二个结合位点包含一个没有明显二级结构的富含嘧啶的必需区域。竞争实验表明，与这两个结合位点形成的复合物是由单一的p57物种形成的。该蛋白也与其他小RNA病毒的5'非翻译区结合。对口蹄疫病毒RNA进行足迹分析的结果表明，翻译起始复合物中还有其他细胞因子参与。
