Gongadze G M, Perederina A A, Meshcheriakov V A, Fedorov R V, Moskalenko S E, Rak A V, Serganov A A, Shcherbakov D V, Nikonov S V, Garber M B
Mol Biol (Mosk). 2001 Jul-Aug;35(4):610-6.
Three 5S rRNA-binding ribosomal proteins (L5, L18, TL5) of extremely thermophilic bacterium Thermus thermophilus have earlier been isolated. Structural analysis of their complexes with rRNA requires identification of their binding sites in the 5S rRNA. Previously, a TL5-binding site has been identified, a TL5-RNA complex crystallized, and its structure determined to 2.3 A. The sites for L5 and L18 were characterized, and two corresponding 5S rRNA fragments constructed. Of these, a 34-nt fragment specifically interacted with L5, and a 55-nt fragment interacted with L5, L18, and with both proteins. The 34-nt fragment-L5 complex was crystallized; the crystals are suitable for high-resolution X-ray analysis.
嗜热栖热菌的三种与5S核糖体RNA结合的核糖体蛋白（L5、L18、TL5）此前已被分离出来。对它们与核糖体RNA复合物的结构分析需要确定它们在5S核糖体RNA中的结合位点。此前，已鉴定出一个TL5结合位点，使TL5-RNA复合物结晶，并将其结构解析至2.3埃。对L5和L18的结合位点进行了表征，并构建了两个相应的5S核糖体RNA片段。其中，一个34个核苷酸的片段与L5特异性相互作用，一个55个核苷酸的片段与L5、L18以及这两种蛋白都相互作用。34个核苷酸的片段-L5复合物结晶；这些晶体适用于高分辨率X射线分析。
