Purohit P, Stern S
Program in Molecular Medicine, UMASS Medical Center, Worcester 01605.
Nature. 1994 Aug 25;370(6491):659-62. doi: 10.1038/370659a0.
It is now generally accepted that 16S and 23S ribosomal RNA play important roles in the decoding and peptidyl transferase activities of ribosomes. Despite their complex structures and numerous associated proteins it is possible that small domains of these rRNAs can fold and function autonomously, particularly those that appear devoid of protein interactions. One candidate for such a domain is the decoding region, located near the 3' end of 16S rRNA (Fig. 1a, b). Consistent with this hypothesis, aminoglycoside antibiotics that interact with the decoding region in 30S subunits interact with other RNAs in the absence of proteins. In addition, certain activities of self-splicing introns, at least superficially, resemble translational decoding. We report here that an oligoribonucleotide analogue of the decoding region interacts with both antibiotic and RNA ligands of the 30S subunit in a manner that correlates with normal subunit function. The activities of the decoding region analogue suggest that the intimidating structural complexity of the ribosome can be, to some degree, circumvented.
现在人们普遍认为，16S和23S核糖体RNA在核糖体的解码和肽基转移酶活性中发挥着重要作用。尽管它们结构复杂且有众多相关蛋白，但这些rRNA的小结构域有可能自主折叠并发挥功能，特别是那些似乎没有蛋白质相互作用的结构域。这样一个结构域的一个候选者是位于16S rRNA 3'端附近的解码区域（图1a、b）。与这一假设一致的是，与30S亚基中的解码区域相互作用的氨基糖苷类抗生素在没有蛋白质的情况下与其他RNA相互作用。此外，自我剪接内含子的某些活性至少在表面上类似于翻译解码。我们在此报告，解码区域的寡核糖核苷酸类似物以与正常亚基功能相关的方式与30S亚基的抗生素和RNA配体相互作用。解码区域类似物的活性表明，核糖体令人生畏的结构复杂性在某种程度上是可以规避的。
