Two cellular proteins that interact with a stem loop in the simian hemorrhagic fever virus 3′(+)NCR RNA
Two cellular proteins that interact with a stem loop in the simian hemorrhagic fever virus 3′(+)NCR RNA
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DOI：
10.1016/j.virusres.2004.11.014
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发表时间：
2005-05-01
期刊：
影响因子：
5
通讯作者：
Brinton, MA
中科院分区：
文献类型：
--
作者：
Maines, TR;Young, M;Brinton, MA
猴出血热病毒（simianhemorrhagicfever virus，SHFV）正链基因组RNA的3 '末端起始于全长和亚基因组负链RNA。SHFV 3 '（+）非编码区（NCR）长76 nt，形成茎环（SL）结构，经核糖核酸酶结构探针证实。两种细胞蛋白p56和p42与由SHFV 3 '（+）NCR RNA组成的探针特异性结合。动脉炎病毒属另外两个成员的3 '（+）NCR RNA与两种相同大小的细胞蛋白特异性相互作用。p56被鉴定为聚嘧啶片段结合蛋白（PTB），p42被鉴定为果糖二磷酸醛缩酶A。PTB结合位点被定位到SHFV 3 ' SL结构的末端环和凸起区域。病毒RNA中PTB结合位点的缺失显著降低PTB结合活性，表明这两个位点都是有效结合该蛋白所必需的。SHFV 3 ' SL结构顶部的变化消除了醛缩酶结合，表明该蛋白的结合位点位于SL顶部附近。这些细胞蛋白可能在基因组3'NCR的功能调节中发挥作用。(c)2004 Elsevier B.V.保留所有权利。
Both full-length and subgenomic negative-strand RNAs are initiated at the 3 ' terminus Of the positive-strand genomic RNA of the arterivirus, simian hemorrhagic fever virus (SHFV). The SHFV 3 '(+) non-coding region (NCR) is 76 nts in length and forms a stem loop (SL) Structure that was confirmed by ribonuclease structure probing. Two cell proteins, p56 and p42, bound specifically to a probe consisting of the SHFV 3 '(+)NCR RNA. The 3 '(+)NCR RNAs of two additional members of the arterivirus genus specifically interacted with two cell proteins of the same size. p56 was identified as polypyrimidine tract-binding protein (PTB) and p42 was identified as fructose bisphosphate aldolase A. PTB binding sites were mapped to a terminal loop and to a bulged region of the SHFV 3 ' SL structure. Deletion of either of the PTB binding sites in the viral RNA significantly reduced PTB binding activity, Suggesting that both sites are required for efficient binding of this protein. Changes in the top portion of the SHFV 3 ' SL structure eliminated aldolase binding, suggesting, that the binding site for this protein is located near the top of the SL. These cell proteins may play roles in regulating the functions of the genomic 3 ' NCR. (c) 2004 Elsevier B.V. All rights reserved.