Christensen T, Johnsen M, Fiil N P, Friesen J D
EMBO J. 1984 Jul;3(7):1609-12. doi: 10.1002/j.1460-2075.1984.tb02018.x.
We have carried out measurements of the stable binding of the ribosomal protein (r-protein) complex L10-L7/L12 to mutant forms of the mRNA leader of the rplJ operon of Escherichia coli. One of the point mutations, base 1548, which lies within the L10-L7/L12-protected region, almost completely abolishes in vitro formation of a stable complex of L10-L7/L12 with rplJ mRNA leader, and a second point mutation, base 1634, strongly reduces it. These observations constitute strong support for the proposition that L10-L7/L12 binds to the rplJ leader in bringing about translational feedback. To account for the action of these and other mutations, and to explain the mechanism of translation feedback inhibition, we suggest a secondary structure model involving alternate forms of the rplJ mRNA leader.
我们已经对核糖体蛋白(r-蛋白)复合物L10-L7/L12与大肠杆菌rplJ操纵子mRNA前导序列的突变形式之间的稳定结合进行了测量。其中一个点突变,即位于L10-L7/L12保护区域内的第1548位碱基,几乎完全消除了L10-L7/L12与rplJ mRNA前导序列在体外形成稳定复合物的能力,而另一个点突变,第1634位碱基,则显著降低了这种能力。这些观察结果有力地支持了L10-L7/L12在实现翻译反馈时与rplJ前导序列结合的观点。为了解释这些及其他突变的作用,并阐明翻译反馈抑制的机制,我们提出了一个涉及rplJ mRNA前导序列交替形式的二级结构模型。