Bommer U A, Stahl J, Henske A, Lutsch G, Bielka H
Academy of Sciences of the GDR, Department of Cell Physiology, Berlin-Buch.
FEBS Lett. 1988 Jun 6;233(1):114-8. doi: 10.1016/0014-5793(88)81366-8.
Monospecific polyclonal antibodies against seven proteins of the 40 S subunit of rat liver ribosomes were used to identify ribosomal proteins involved in interaction with initiation factor eIF-2 in the quaternary initiation complex [eIF-2 X GMPPCP X [3H]Met-tRNAf X 40 S ribosomal subunit]. Dimeric immune complexes of 40 S subunits mediated by antibodies against ribosomal proteins S3a, S13/16, S19 and S24 were found to be unable to bind the ternary initiation complex [eIF-2 X GMPPCP X [3H]Met-tRNAf]. In contrast, 40 S dimers mediated by antibodies against proteins S2, S3 and S17 were found to bind the ternary complex. Therefore, from the ribosomal proteins tested, only proteins S3a, S13/16, S19 and S24 are concluded to be involved in eIF-2 binding to the 40 S subunit.
利用针对大鼠肝脏核糖体40 S亚基七种蛋白质的单特异性多克隆抗体，来鉴定在四级起始复合物[eIF-2 X GMPPCP X [3H]Met-tRNAf X 40 S核糖体亚基]中与起始因子eIF-2相互作用的核糖体蛋白质。发现由针对核糖体蛋白质S3a、S13/16、S19和S24的抗体介导的40 S亚基二聚体免疫复合物无法结合三元起始复合物[eIF-2 X GMPPCP X [3H]Met-tRNAf]。相反，发现由针对蛋白质S2、S3和S17的抗体介导的40 S二聚体能够结合三元复合物。因此，从所测试的核糖体蛋白质中得出结论，只有蛋白质S3a、S13/16、S19和S24参与eIF-2与40 S亚基的结合。
