Amons R, Muranova T A, Rykunova A I, Eliseikina I A, Sedelnikova S E
Department of Medical Biochemistry, University of Leiden, The Netherlands.
J Protein Chem. 1993 Dec;12(6):725-34. doi: 10.1007/BF01024930.
The primary structure of the 23S rRNA binding ribosomal protein L1 from the 50S ribosomal subunit of Thermus thermophilus ribosomes has been elucidated by direct protein sequencing of selected peptides prepared by enzymatic and chemical cleavage of the intact purified protein. The polypeptide chain contains 228 amino acids and has a calculated molecular mass of 24,694 D. A comparison with the primary structures of the corresponding proteins from Escherichia coli and Bacillus stearothermophilus reveals a sequence homology of 49% and 58%, respectively. With respect to both proteins, L1 from T. thermophilus contains particularly less Ala, Lys, Gln, and Val, whereas its content of Glu, Gly, His, Ile, and Arg is higher. In addition, two fragments obtained by limited proteolysis of the intact, unmodified protein were characterized.
嗜热栖热菌核糖体50S亚基中与23S rRNA结合的核糖体蛋白L1的一级结构，已通过对完整纯化蛋白经酶切和化学裂解制备的选定肽段进行直接蛋白质测序得以阐明。该多肽链含有228个氨基酸，计算分子量为24,694 D。与来自大肠杆菌和嗜热脂肪芽孢杆菌的相应蛋白的一级结构比较显示，序列同源性分别为49%和58%。相对于这两种蛋白，嗜热栖热菌的L1含有特别少的丙氨酸、赖氨酸、谷氨酰胺和缬氨酸，而其谷氨酸、甘氨酸、组氨酸、异亮氨酸和精氨酸的含量较高。此外，还对完整未修饰蛋白经有限蛋白酶解得到的两个片段进行了表征。
