Nowotny V, Nierhaus K H
Proc Natl Acad Sci U S A. 1982 Dec;79(23):7238-42. doi: 10.1073/pnas.79.23.7238.
An rRNA-binding protein that binds to the rRNA independently of other proteins during the course of ribosomal assembly is termed "assembly initiator protein." In spite of the large number of rRNA-binding proteins (more than 17 out of 32 proteins have been identified in the case of the large ribosomal subunit), only a very small number of proteins should actually initiate ribosomal assembly for theoretical reasons. Here we demonstrate that only two of the L proteins derived from the large subunit (50S) function as assembly initiator proteins. Two different techniques are used to identify these initiator proteins: reconstitution experiments with purified proteins and pulse-chase experiments during in vitro assembly. Both methods independently identify L24 and L3 as initiator proteins for the 50S assembly. The existence of two initiator proteins (not just one) resolves an apparent contradiction--namely, that on the one hand, rRNA is synthesized in excess under unfavorable growth conditions, whereas on the other hand, rRNA-binding proteins should be available for translational control.
一种在核糖体组装过程中独立于其他蛋白质与核糖体RNA(rRNA)结合的rRNA结合蛋白被称为“组装起始蛋白”。尽管存在大量的rRNA结合蛋白(在大核糖体亚基的情况下,已鉴定出32种蛋白中的17种以上),但出于理论原因,实际上只有极少数蛋白质应该启动核糖体组装。在这里,我们证明了来自大亚基(50S)的L蛋白中只有两种作为组装起始蛋白发挥作用。使用两种不同的技术来鉴定这些起始蛋白:用纯化蛋白进行的重组实验和体外组装过程中的脉冲追踪实验。两种方法都独立地将L24和L3鉴定为50S组装的起始蛋白。两种起始蛋白(而非仅一种)的存在解决了一个明显的矛盾,即一方面,在不利的生长条件下rRNA会过量合成,而另一方面,rRNA结合蛋白应可用于翻译控制。