期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1977
卷号：74
期号：7
页码：2706-2709
DOI：10.1073/pnas.74.7.2706
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
