Sm样Hfq蛋白的RNA伴侣活性。
RNA chaperone activity of the Sm-like Hfq protein.
作者信息
Moll Isabella, Leitsch David, Steinhauser Tanja, Bläsi Udo
机构信息
Institute of Microbiology and Genetics, Vienna Biocenter, Dr. Bohrgasse 9, 1030 Vienna, Austria.
出版信息
EMBO Rep. 2003 Mar;4(3):284-9. doi: 10.1038/sj.embor.embor772.
Abstract
The Escherichia coli Sm-like host factor I (Hfq) protein is thought to function in post-transcriptional regulation by modulating the function of small regulatory RNAs. Hfq also interferes with ribosome binding on E. coli ompA messenger RNA, indicating that Hfq also interacts with mRNAs. In this study, we have used stimulation of group I intron splicing in vivo and a modified in vitro toeprinting assay to determine whether Hfq acts as an RNA chaperone. Hfq was able to rescue an RNA 'folding trap' in a splicing defective T4 bacteriophage td gene in vivo. Enzymatic analysis showed that Hfq affects the accessibility of the ompA start codon, as well as other bases within the ribosome-binding site, explaining its negative effect on ribosome binding. We also show that the Hfq-induced structural changes in ompA mRNA are maintained after proteolytic digestion of the protein, which classifies Hfq as an RNA chaperone.
摘要
大肠杆菌Sm样宿主因子I（Hfq）蛋白被认为通过调节小调节RNA的功能在转录后调控中发挥作用。Hfq还会干扰核糖体与大肠杆菌ompA信使RNA的结合，这表明Hfq也与mRNA相互作用。在本研究中，我们利用体内I组内含子剪接的刺激以及改良的体外足迹分析来确定Hfq是否作为一种RNA伴侣发挥作用。Hfq能够在体内挽救剪接缺陷型T4噬菌体td基因中的RNA“折叠陷阱”。酶分析表明，Hfq会影响ompA起始密码子以及核糖体结合位点内其他碱基的可及性，这解释了其对核糖体结合的负面影响。我们还表明，在对该蛋白进行蛋白水解消化后，Hfq诱导的ompA mRNA结构变化得以维持，这将Hfq归类为一种RNA伴侣。
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