Footprinting the sites of interaction of antibiotics with catalytic group I intron RNA.
Footprinting the sites of interaction of antibiotics with catalytic group I intron RNA.
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DOI：
10.1126/science.8502993
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发表时间：
1993-06
期刊：
影响因子：
56.9
通讯作者：
U. Ahsen;H. Noller
中科院分区：
文献类型：
--
作者：
U. Ahsen;H. Noller
先前已显示氨基糖苷类翻译抑制剂抑制I组内含子的体外自剪接。噬菌体T4衍生的sunY内含子的化学探测表明，新霉素，链霉素，和相关抗生素保护的N-7位置的G96，一个普遍保守的鸟嘌呤在剪接反应中的鸟苷辅因子的结合位点。抗生素还破坏了结构接触，这些结构接触被认为是使内含子的5'切割位点接近催化核心。相反，严格竞争性抑制剂脱氧鸟苷和精氨酸仅保护G96的N-7位。这些结果与先前观察到的氨基糖苷类对16 S核糖体RNA的保护之间的相似之处提高了I组内含子剪接和核糖体转移RNA选择涉及类似RNA结构基序的可能性。
Aminoglycoside inhibitors of translation have been shown previously to inhibit in vitro self-splicing by group I introns. Chemical probing of the phage T4-derived sunY intron shows that neomycin, streptomycin, and related antibiotics protected the N-7 position of G96, a universally conserved guanine in the binding site for the guanosine cofactor in the splicing reaction. The antibiotics also disrupted structural contacts that have been proposed to bring the 5' cleavage site of the intron into proximity to the catalytic core. In contrast, the strictly competitive inhibitors deoxyguanosine and arginine protected only the N-7 position of G96. Parallels between these results and previously observed protection of 16S ribosomal RNA by aminoglycosides raise the possibility that group I intron splicing and transfer RNA selection by ribosomes involve similar RNA structural motifs.