Elisekina I A, Avliiakulov N K, Grishkovskaia I B, Muranova T A, Sedel'nikova S E, Garber M B
Biokhimiia. 1996 Nov;61(11):2040-4.
Fragments of the ribosomal protein L1 from Thermus thermophilus were obtained by limited trypsinolysis and spontaneous proteolysis. Binding of the intact L1 and its proteolytic fragments to 23S ribosomal RNA was studied. First eight N-terminal amino acids are important for RNA binding because protein L1 lacking these amino acids exhibits reduced 23S rRNA binding. Additional cleavage of the polypeptide chain between residues 36 and 37 completely abolishes RNA binding. Comparison of these data with recently determined structure of protein L1 from T. thermophilus suggests the nature of interactions which can determine specific and strong association of the protein L1 with 23S rRNA.
嗜热栖热菌核糖体蛋白L1的片段通过有限的胰蛋白酶消化和自发蛋白水解获得。研究了完整的L1及其蛋白水解片段与23S核糖体RNA的结合。前八个N端氨基酸对RNA结合很重要，因为缺少这些氨基酸的蛋白L1与23S rRNA的结合能力降低。多肽链在第36和37位残基之间的进一步切割完全消除了RNA结合。将这些数据与最近确定的嗜热栖热菌蛋白L1的结构进行比较，揭示了决定蛋白L1与23S rRNA特异性和强结合的相互作用的本质。
