Torres-Larios Alfredo, Dock-Bregeon Anne-Catherine, Romby Pascale, Rees Bernard, Sankaranarayanan Rajan, Caillet Joel, Springer Mathias, Ehresmann Chantal, Ehresmann Bernard, Moras Dino
Laboratoire de Biologie et Génomique Structurales, IGBMC, BP163, 67404 Illkirch Cedex, France.
Nat Struct Biol. 2002 May;9(5):343-7. doi: 10.1038/nsb789.
Escherichia coli threonyl-tRNA synthetase (ThrRS) represses the translation of its own messenger RNA by binding to an operator located upstream of the initiation codon. The crystal structure of the complex between the core of ThrRS and the essential domain of the operator shows that the mRNA uses the recognition mode of the tRNA anticodon loop to initiate binding. The final positioning of the operator, upon which the control mechanism is based, relies on a characteristic RNA motif adapted to the enzyme surface. The finding of other thrS operators that have this conserved motif leads to a generalization of this regulatory mechanism to a subset of Gram-negative bacteria.
大肠杆菌苏氨酰 - tRNA合成酶（ThrRS）通过与起始密码子上游的一个操纵子结合来抑制其自身信使RNA的翻译。ThrRS核心与操纵子必需结构域之间复合物的晶体结构表明，mRNA利用tRNA反密码子环的识别模式来启动结合。基于此控制机制的操纵子的最终定位依赖于一个适应酶表面的特征性RNA基序。发现其他具有这种保守基序的thrS操纵子，使得这种调控机制推广到了一部分革兰氏阴性菌中。
