Tate W P, McCaughan K K, Kastner B, Trotman C N, Stoffler-Meilicke M, Stoffler G
Department of Biochemistry, University of Otago, Dunedin, New Zealand.
Biochem Int. 1988 Jul;17(1):179-86.
A domain of the 30S subunit of the Escherichia coli ribosome is in close contact with the release factor when it binds to the 70S particle during the termination of protein biosynthesis. This has been characterised using antibodies specific for the individual proteins of the small ribosomal subunit. Most antibodies do not affect the release factor-mediated reactions but those against S3, S4, S5 and S10 are inhibitory. These proteins are clustered on the lower head and the upper part of the small lobe of the subunit. The regions of these features which are near the interface between the two subunits in the 70S ribosome are known to be close to the base of the stalk of the 50S subunit.
在蛋白质生物合成终止过程中，当大肠杆菌核糖体30S亚基的一个结构域与释放因子结合到70S颗粒上时，它会与释放因子紧密接触。这已通过针对小核糖体亚基各个蛋白质的特异性抗体进行了表征。大多数抗体不影响释放因子介导的反应，但针对S3、S4、S5和S10的抗体具有抑制作用。这些蛋白质聚集在亚基小叶片的下部头部和上部。已知在70S核糖体中两个亚基之间界面附近的这些特征区域靠近50S亚基柄的基部。
