Brigotti M, Rambelli F, Zamboni M, Montanaro L, Sperti S
Dipartimento di Patologia sperimentale dell'Università di Bologna, Italy.
Biochem J. 1989 Feb 1;257(3):723-7. doi: 10.1042/bj2570723.
alpha-Sarcin from Aspergillus giganteus and the ribosome-inactivating proteins (RIPs) from higher plants inactivate the 60 S ribosomal subunit. The former is an RNAase, whereas RIPs are N-glycosidases. The site of cleavage of RNA and that of N-glycosidic depurinization are at one nucleotide distance in 28 S rRNA [Endo & Tsurugi (1987) J. Biol. Chem. 262, 8128-8130]. The effect of alpha-sarcin and that of RIPs on the interaction of elongation factors with Artemia salina (brine shrimp) ribosomes have been investigated. alpha-Sarcin inhibits both the EF1 (elongation factor 1)-dependent binding of aminoacyl-tRNA and the GTP-dependent binding of EF2 (elongation factor 2) to ribosomes, whereas two of the RIPs tested, ricin from Ricinus communis (castor bean) and volkensin from Adenia volkensii (kilyambiti), inhibit only the latter reaction. EF2 protects ribosomes from inactivation by both alpha-sarcin and ricin. The EF1-binding site is affected only by alpha-sarcin. The sensitivity of this site to alpha-sarcin is increased by pretreatment of ribosomes with ricin. A. salina ribosomes were highly resistant to the third RIP tested, namely gelonin from Gelonium multiflorum. All four proteins tested have, however, a comparable activity on the rabbit reticulocyte-lysate system.
来自巨大曲霉的α-肌动蛋白和高等植物的核糖体失活蛋白(RIPs)可使60 S核糖体亚基失活。前者是一种RNA酶,而RIPs是N-糖苷酶。RNA的切割位点和N-糖苷脱嘌呤位点在28 S rRNA中相隔一个核苷酸距离[远藤和鹤木(1987年)《生物化学杂志》262,8128 - 8130]。已经研究了α-肌动蛋白和RIPs对卤虫核糖体与延伸因子相互作用的影响。α-肌动蛋白既抑制氨基酰-tRNA依赖于延伸因子1(EF1)的结合,也抑制延伸因子2(EF2)依赖于GTP的与核糖体的结合,而所测试的两种RIPs,即来自蓖麻的蓖麻毒素和来自腺叶藤属的伏肯辛,仅抑制后一种反应。EF2可保护核糖体不被α-肌动蛋白和蓖麻毒素失活。EF1结合位点仅受α-肌动蛋白影响。用蓖麻毒素预处理核糖体可增加该位点对α-肌动蛋白的敏感性。卤虫核糖体对所测试的第三种RIP,即来自多花巴豆的巴豆球蛋白具有高度抗性。然而,所测试的所有四种蛋白质在兔网织红细胞裂解物系统中具有相当的活性。