Tsiboli P, Herfurth E, Choli T
Aristotle University of Thessaloniki, School of Chemistry, Laboratory of Biochemistry, Greece.
Eur J Biochem. 1994 Nov 15;226(1):169-77. doi: 10.1111/j.1432-1033.1994.tb20038.x.
The total protein mixture of the 30S subunit (TP-30) of the bacterium Thermus thermophilus has been purified using reverse-phase HPLC and the proteins obtained were identified both by means of two-dimensional polyacrylamide gel electrophoresis as well as by amino-terminal amino acid microsequence analysis. The proteins are numbered according to their primary structural similarity with known prokaryotic ribosomal proteins. Eight of them, namely proteins S6, S7, S9, S10, S14, S15, S16 and S17 run at different positions in the two-dimensional gel electrophoresis system to those suggested [Sedelnikova, S. C., Agalarov, M. B., Garber, M. & Yusupov, M. M. (1987) FEBS Lett. 220, 227-230]. All characterized proteins are homologous to known ribosomal proteins from other species, except for a small basic protein which shows homology only to a ribosomal protein from spinach chloroplasts [Choli, T., Franceschi, F., Yonath, A. & Wittmann-Leibold, B. (1993) Biol. Chem. Hoppe-Seyler 374, 377-383; Subramanian, A.-R. (1984) Trends Biochem. Sci. 9, 491-494].
嗜热栖热菌30S亚基的总蛋白混合物（TP-30）已通过反相高效液相色谱法纯化，所得蛋白质通过二维聚丙烯酰胺凝胶电泳以及氨基末端氨基酸微序列分析进行了鉴定。这些蛋白质根据它们与已知原核核糖体蛋白质的一级结构相似性进行编号。其中八种蛋白质，即蛋白质S6、S7、S9、S10、S14、S15、S16和S17，在二维凝胶电泳系统中的迁移位置与之前报道的不同[Sedelnikova, S. C., Agalarov, M. B., Garber, M. & Yusupov, M. M. (1987) FEBS Lett. 220, 227 - 230]。除了一种小的碱性蛋白质仅与菠菜叶绿体的一种核糖体蛋白质具有同源性外[Choli, T., Franceschi, F., Yonath, A. & Wittmann-Leibold, B. (1993) Biol. Chem. Hoppe-Seyler 374, 377 - 383; Subramanian, A.-R. (1984) Trends Biochem. Sci. 9, 491 - 494]，所有已鉴定的蛋白质都与其他物种的已知核糖体蛋白质同源。
