真核生物延伸因子EF-1和EF-2与核糖体相互作用的构象控制。
Conformational control of the interaction of eukaryotic elongation factors EF-1 and EF-2 with ribosomes.
作者信息
Nombela C, Ochoa S
出版信息
Proc Natl Acad Sci U S A. 1973 Dec;70(12):3556-60. doi: 10.1073/pnas.70.12.3556.
Abstract
As in the case with prokaryotic systems, Artemia salina elongation factors EF-1 and EF-2 interact with a common site or with closely overlapping sites on the Artemia ribosome. This feature of ribosomal design must restrict interaction with the ribosome to only one of the factors at alternating steps of chain elongation. In support of this view we find that EF-1, but not EF-2, interacts with the post-translocation ribosome, whereas the reverse is true of the pre-translocation ribosome. Conformational changes probably account for the alternating selectivity of the translating ribosome for each elongation factor.
摘要
与原核生物系统的情况一样，卤虫的延伸因子EF-1和EF-2与卤虫核糖体上的一个共同位点或紧密重叠的位点相互作用。核糖体设计的这一特征必然会在链延伸的交替步骤中将与核糖体的相互作用限制在仅一种因子上。支持这一观点的是，我们发现EF-1（而非EF-2）与转位后的核糖体相互作用，而转位前的核糖体情况则相反。构象变化可能解释了翻译核糖体对每种延伸因子的交替选择性。
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