Sköld S E
Eur J Biochem. 1982 Oct;127(2):225-9. doi: 10.1111/j.1432-1033.1982.tb06859.x.
Ribosomal proteins situated at or near the binding site of elongation factor G (EF-G) on the Escherichia coli ribosome have been identified by use of the bifunctional, cleavable cross-linker, dimethyl-4,9-diaza-5,8-dioxo-6,7-dihydroxy-dodecanebisimidate. Five different bimolecular EF-G x ribosomal-protein complexes were isolated electrophoretically. The ribosomal proteins found in each of these complexes were identified as the 50-S-subunit proteins L6, L7/L12 and L14 and the 30-S-subunit proteins S12 and S19. In the presence of thiostrepton, which prevents binding of EF-G to the ribosome, there was a considerable decrease in the yield of each of these cross-linked complexes. The data suggest that EF-G is bound close to the ribosomal subunit interface.
利用双功能、可裂解的交联剂二甲基-4,9-二氮杂-5,8-二氧代-6,7-二羟基十二烷双亚氨酸酯，已鉴定出位于大肠杆菌核糖体上延伸因子G（EF-G）结合位点处或附近的核糖体蛋白。通过电泳分离出了五种不同的双分子EF-G与核糖体蛋白复合物。在这些复合物中发现的核糖体蛋白被鉴定为50-S亚基蛋白L6、L7/L12和L14以及30-S亚基蛋白S12和S19。在硫链丝菌素存在的情况下，硫链丝菌素会阻止EF-G与核糖体结合，这些交联复合物中的每一种产量都大幅下降。数据表明EF-G结合在核糖体亚基界面附近。
