Hausmann Corinne D, Ibba Michael
Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210-1292, USA.
FEBS Lett. 2008 Jun 25;582(15):2178-82. doi: 10.1016/j.febslet.2008.05.043. Epub 2008 Jun 5.
Methanothermobacter thermautotrophicus contains a multi-aminoacyl-tRNA synthetase complex (MSC) of LysRS, LeuRS and ProRS. Elongation factor (EF) 1A also associates to the MSC, with LeuRS possibly acting as a core protein. Analysis of the MSC revealed that LysRS and ProRS specifically interact with the idiosyncratic N- and C- termini of LeuRS, respectively. EF-1A instead interacts with the inserted CP1 proofreading domain, consistent with models for post-transfer editing by class I synthetases such as LeuRS. Together with previous genetic data, these findings show that LeuRS plays a central role in mediating interactions within the archaeal MSC by acting as a core scaffolding protein.
嗜热自养甲烷杆菌含有由赖氨酸氨酰-tRNA合成酶（LysRS）、亮氨酸氨酰-tRNA合成酶（LeuRS）和脯氨酸氨酰-tRNA合成酶（ProRS）组成的多氨酰-tRNA合成酶复合体（MSC）。延伸因子（EF）1A也与该MSC相关联，其中LeuRS可能作为核心蛋白。对该MSC的分析表明，LysRS和ProRS分别与LeuRS特异的N端和C端相互作用。相反，EF-1A与插入的CP1校对结构域相互作用，这与I类合成酶（如LeuRS）的转移后编辑模型一致。与先前的遗传学数据一起，这些发现表明LeuRS通过作为核心支架蛋白在介导古菌MSC内的相互作用中发挥核心作用。
