SsrA介导的LacI标签化与蛋白水解作用及其在乳糖操纵子调控中的作用。
SsrA-mediated tagging and proteolysis of LacI and its role in the regulation of lac operon.
作者信息
Abo T, Inada T, Ogawa K, Aiba H
机构信息
Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa, Nagoya 464-8602, Japan.
出版信息
EMBO J. 2000 Jul 17;19(14):3762-9. doi: 10.1093/emboj/19.14.3762.
Abstract
SsrA RNA of Escherichia coli, also known as 10Sa RNA or tmRNA, acts both as tRNA and mRNA when ribosomes are paused at the 3' end of an mRNA lacking a stop codon. This process, referred to as trans-translation, leads to the addition of a short peptide tag to the C-terminus of the incomplete nascent polypeptide. The tagged polypeptide is then degraded by C-terminal-specific proteases. Here, we focused on endogenous targets for the SsrA system and on a potential regulatory role of SsrA RNA. First, we show that trans-translation events occur frequently in normally growing E. COLI: cells. More specifically, we report that the lacI mRNA encoding Lac repressor (LacI) is a specific natural target for trans-translation. The binding of LacI to the lac operators results in truncated lacI mRNAs that are, in turn, recognized by the SsrA system. The SsrA-mediated tagging and proteolysis of LacI appears to play a role in cellular adaptation to lactose availability by supporting a rapid induction of lac operon expression.
摘要
大肠杆菌的SsrA RNA，也被称为10Sa RNA或tmRNA，当核糖体在缺乏终止密码子的mRNA的3'末端暂停时，它同时充当tRNA和mRNA。这个过程被称为反式翻译，导致在不完整的新生多肽的C末端添加一个短肽标签。然后，被标记的多肽被C末端特异性蛋白酶降解。在这里，我们关注SsrA系统的内源性靶标以及SsrA RNA的潜在调节作用。首先，我们表明反式翻译事件在正常生长的大肠杆菌细胞中频繁发生。更具体地说，我们报告编码Lac阻遏物（LacI）的lacI mRNA是反式翻译的一个特定天然靶标。LacI与lac操纵子的结合导致截短的lacI mRNA，进而被SsrA系统识别。SsrA介导的LacI标记和蛋白水解似乎通过支持lac操纵子表达的快速诱导在细胞对乳糖可用性的适应中发挥作用。
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