THE SECONDARY STRUCTURE OF THE PROTEIN L1 BINDING REGION OF RIBOSOMAL 23S RNA - HOMOLOGIES WITH PUTATIVE SECONDARY STRUCTURES OF THE L11 MESSENGER-RNA AND OF A REGION OF MITOCHONDRIAL 16S-RRNA

THE SECONDARY STRUCTURE OF THE PROTEIN L1 BINDING REGION OF RIBOSOMAL 23S RNA - HOMOLOGIES WITH PUTATIVE SECONDARY STRUCTURES OF THE L11 MESSENGER-RNA AND OF A REGION OF MITOCHONDRIAL 16S-RRNA
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DOI:
10.1093/nar/9.2.293
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发表时间:
1981-01-01
影响因子:
14.9
通讯作者:
EBEL, JP
EBEL, JP
中科院分区:
生物学2区
文献类型:
--
作者:
BRANLANT, C;KROL, A;EBEL, JP

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E.大肠杆菌蛋白L1和P. vulgavis23S RNA。我们确定了RNA区域的一级结构,该区域在RNase消化该复合物后仍与蛋白L1相关。我们还鉴定了这一RNA区域分别对T1、S1和Naja oxiananuclease digestion高度敏感的位点。将这些结果与以前用E. coliandB.嗜热脂肪菌23S RNA,我们假设的蛋白质L1结合区的细菌23S RNA的一般结构。小鼠和人的mit 16S rRNA以及非洲爪蟾和四膜虫的28S rRNA都含有与E. coli23SrRNA区域位于L1结合位点之前。该序列后的16S rRNA区域具有潜在的二级结构,与细菌23S rRNA的L1相关区域具有共同特征。L11mRNA的5′端区域也具有几个序列潜在的二级结构,与23SrRNA的蛋白L1结合区显示出惊人的同源性,这可能解释了蛋白L1如何作为翻译阻遏物起作用。其中一个L11mRNA推定结构具有与细菌23SrRNA的L1相关区域和mit 16SrRNA的相应区域共同的特征。
An heterologous complex was formed betweenE. coliprotein L1 andP. vulgavis23S RNA. We determined the primary structure of the RNA region which remained associated with protein L1 after RNase digestion of this complex. We also identified the loci of this RNA region which are highly susceptible to T1, S1 andNaja oxiananuclease digestions respectively. By comparison of these results with those previously obtained with the homologous regions ofE. coliandB. stearothermophilus23S RNAs, we postulate a general structure for the protein L1 binding region of bacterial 23S RNA. Both mouse and human mit 16S rRNAs andXenopus laevisandTetrahymena28S rRNAs contain a sequence similarto theE. coli23S rRNA region preceding the L1 binding site. The region ofmit 16S rRNA which follows this sequence has a potential secondary structure bearing common features with the L1-associated region of bacterial 23S rRNA. The 5′- end region of the L11 mRNA also has several sequence potential secondary structures displaying striking homologies with the protein L1 binding region of 23S rRNA and this probably explains how protein L1 functions as a translational repressor. One of the L11 mRNA putative structures bears the features common to both the L1-associated region of bacterial 23S rRNA andthe corresponding region of mit 16S rRNA.