Glick B R, Chládek S, Ganoza M C
Eur J Biochem. 1979 Jun;97(1):23-8. doi: 10.1111/j.1432-1033.1979.tb13081.x.
Elongation factor EF-P is a soluble protein that stimulates peptide bond synthesis catalyzed by the 50-S ribosomal subunit. This factor was previously identified and characterized based on its ability to promote the synthesis of formylmethionine-puromycin. In the present work, we tested the ability of EF-P to promote peptide bond synthesis between ribosome-bound fMet-tRNA and several analogues of the 3' terminus of aminoacyl-tRNA, i.e. the cytidylyl(3'-5')-[2'(3')-O-L-aminoacyladenosines]. EF-P promoted synthesis to the greatest extent with certain acceptors which were otherwise inefficient in the peptidyl transferase reaction. This activity of EF-P could not be replaced by the other soluble proteins known to be involved in polypeptide synthesis, such as EF-Tu, EF-Ts and EF-G. One role of EF-P in protein synthesis may be to allow peptide bond synthesis to occur more efficiently with some aminoacyl-tRNAs that are poor acceptors for the ribosomal peptidyl transferase.
延伸因子EF-P是一种可溶性蛋白质，可刺激50-S核糖体亚基催化的肽键合成。该因子先前是根据其促进甲酰甲硫氨酸-嘌呤霉素合成的能力来鉴定和表征的。在本研究中，我们测试了EF-P促进核糖体结合的fMet-tRNA与氨酰-tRNA 3'末端的几种类似物（即胞苷酰(3'-5')-[2'(3')-O-L-氨酰腺苷]）之间肽键合成的能力。EF-P与某些在肽基转移酶反应中效率低下的受体一起时，能最大程度地促进合成。EF-P的这种活性不能被已知参与多肽合成的其他可溶性蛋白质（如EF-Tu、EF-Ts和EF-G）所替代。EF-P在蛋白质合成中的一个作用可能是使肽键合成能更有效地与一些对核糖体肽基转移酶来说是较差受体的氨酰-tRNA发生。
