Wrede P, Erdmann V A
Proc Natl Acad Sci U S A. 1977 Jul;74(7):2706-9. doi: 10.1073/pnas.74.7.2706.
Reconstitution experiments showed that the two Escherichia coli 5S RNA binding proteins L18 and L25 form a specific complex with yeast 5.8S RNA and not with yeast 5S RNA. The yeast 5.8S RNA-E. coli protein complex was found to exhibit ATPase and GTPase activities that had previously been observed for the E. coli 5S RNA-protein complex. The tetranucleotide UpUpCpG, which is an analog of the tRNA fragment TpsipCpG, interacted strongly with 5S RNA-protein complexes from E. coli and Bacillus stearothermophilus and weakly with yeast 5.8S RNA. UpUpCpG did not bind to E. coli, B. stearothermophilus, or yeast 5S RNA or to the yeast 5.8S RNA-E. coli protein complex. It is suggested that 5.8S RNA evolved from prokaryotic 5S RNA and that the latter two RNAs are related and have similar functions in protein synthesis.
重组实验表明，两种大肠杆菌5S RNA结合蛋白L18和L25与酵母5.8S RNA形成特异性复合物，而不与酵母5S RNA形成复合物。发现酵母5.8S RNA-大肠杆菌蛋白复合物具有先前在大肠杆菌5S RNA-蛋白复合物中观察到的ATP酶和GTP酶活性。四核苷酸UpUpCpG是tRNA片段TpsipCpG的类似物，它与来自大肠杆菌和嗜热脂肪芽孢杆菌的5S RNA-蛋白复合物强烈相互作用，而与酵母5.8S RNA弱相互作用。UpUpCpG不与大肠杆菌、嗜热脂肪芽孢杆菌或酵母的5S RNA结合，也不与酵母5.8S RNA-大肠杆菌蛋白复合物结合。有人提出，5.8S RNA由原核生物的5S RNA进化而来，后两种RNA相关且在蛋白质合成中具有相似功能。
