破碎核糖体：延伸因子EF-G与模拟23S核糖体RNA的肌动蛋白/蓖麻毒素及硫链丝菌素结构域的寡核糖核苷酸的结合
The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA.
作者信息
Munishkin A, Wool I G
机构信息
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
出版信息
Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12280-4. doi: 10.1073/pnas.94.23.12280.
Abstract
An oligoribonucleotide (a 27-mer) that mimics the sarcin/ricin (S/R) domain of Escherichia coli 23S rRNA binds elongation factor EF-G; the Kd is 6.9 microM, whereas for binding to ribosomes it is 0.7 microM. Binding saturates when EF-G and the S/R RNA are equimolar; at saturation 70% of the input RNA is in complexes with EF-G. Binding of EF-G to S/R RNA does not require GTP but is inhibited by GDP; the inhibition by GDP is overcome by GTP. The effects of mutations of the S/R domain nucleotides G2655, A2660, and G2661 suggest that EF-G recognizes the conformation of the RNA rather than the identity of the nucleotides. EF-G also binds to an oligoribonucleotide (an 84-mer) that has the thiostrepton region of 23S rRNA; however, EF-G binds independently to S/R and thiostrepton oligoribonucleotides.
摘要
一种模拟大肠杆菌23S rRNA的肌动蛋白/蓖麻毒素（S/R）结构域的寡核糖核苷酸（27聚体）可结合延伸因子EF-G；其解离常数（Kd）为6.9微摩尔，而与核糖体结合时为0.7微摩尔。当EF-G和S/R RNA等摩尔时，结合达到饱和；在饱和状态下，70%的输入RNA与EF-G形成复合物。EF-G与S/R RNA的结合不需要GTP，但会被GDP抑制；GTP可克服GDP的抑制作用。S/R结构域核苷酸G2655、A2660和G2661的突变效应表明，EF-G识别的是RNA的构象而非核苷酸的身份。EF-G还可结合一种具有23S rRNA硫链丝菌素区域的寡核糖核苷酸（84聚体）；然而，EF-G独立地与S/R和硫链丝菌素寡核糖核苷酸结合。
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The ribosome-in-pieces: binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA.破碎核糖体：延伸因子EF-G与模拟23S核糖体RNA的肌动蛋白/蓖麻毒素及硫链丝菌素结构域的寡核糖核苷酸的结合
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