Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
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DOI：
10.1073/pnas.93.1.76
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发表时间：
1996-01-09
影响因子：
11.1
通讯作者：
Inouye, M
中科院分区：
文献类型：
--
作者：
Jones, PG;Mitta, M;Inouye, M
当培养温度从37 ℃变化到15 ℃时，在大肠杆菌中特异性地诱导了一个70-kDa的蛋白，该蛋白被鉴定为deaD基因的产物（重新命名为csdA）编码DEAD-盒蛋白，此外，在从37 ℃转变到15 ℃后，CsdA仅定位于核糖体组分中，并在15 ℃下生长的细胞中成为主要的核糖体相关蛋白。csdA缺失显着损害细胞生长和一些蛋白质的合成，特别是热休克蛋白的去阻遏，在低温下。发现纯化的CsdA在缺乏ATP的情况下解旋双链RNA，因此，CsdA在热休克蛋白合成的去阻遏中的需求是冷休克诱导的功能，可能由先前在rpoH mRNA中鉴定的二级结构的不稳定介导。
A 70-kDa protein was specifically induced in Escherichia coli when the culture temperature was shifted from 37 to 15 degrees C, The protein was identified to be the product of the deaD gene (reassigned csdA) encoding a DEAD-box protein, Furthermore, after the shift from 37 to 15 degrees C, CsdA was exclusively localized in the ribosomal fraction and became a major ribosomal-associated protein in cells grown at 15 degrees C. The csdA deletion significantly impaired cell growth and the synthesis of a number of proteins, specifically the derepression of heat-shock proteins, at low temperature. Purified CsdA was found to unwind double-stranded RNA in the absence of ATP, Therefore, the requirement: for CsdA in derepression of heat-shock protein synthesis is a cold shock-induced function possibly mediated by destabilization of secondary structures previously identified in the rpoH mRNA.