Ramirez C, Shimmin L C, Dennis P P, Matheson A T
Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
Protein Seq Data Anal. 1991 Aug;4(2):75-9.
The sequences of two ribosomal proteins from two widely divergent species of archaebacteria, Halobacterium cutirubrum and Sulfolobus solfataricus, have been deduced from the structure of their respective genes. These two proteins were found to be equivalent to the L11 and L1 ribosomal proteins of the eubacterium Escherichia coli. Sequence comparison revealed that the archaebacterial L11e (equivalent to E. coli L11) proteins are longer than the eubacterial protein due to a C-terminal extension of about 30 residues. The archaebacterial L11e proteins, like the E. coli L11, are rich in proline residues; most of these are conserved. L11 is the most highly methylated protein in the E. coli ribosome. However, sites of methylation are generally not conserved in the archaebacterial L11e proteins. The region of highest sequence similarity between L11 and the archaebacterial L11e proteins is the N-terminal domain. This domain is believed to interact with release factor 1 during termination of translation. The amino acid sequences of the archaebacterial L1e proteins were compared to the eubacterial E. coli L1 and Bacillus stearothermophilus L1e sequences. The archaebacterial L1e proteins are slightly shorter at both their N- and C-termini. A region of high sequence similarity (7 of 14 residues) occurs near the center of the proteins.
从两种差异很大的古细菌——深红嗜盐菌（Halobacterium cutirubrum）和嗜热栖热菌（Sulfolobus solfataricus）中两种核糖体蛋白的各自基因结构推导出了它们的序列。发现这两种蛋白分别等同于真细菌大肠杆菌（Escherichia coli）的L11和L1核糖体蛋白。序列比较显示，由于约30个残基的C端延伸，古细菌的L11e（等同于大肠杆菌L11）蛋白比真细菌的蛋白更长。古细菌的L11e蛋白与大肠杆菌的L11一样，富含脯氨酸残基；其中大多数是保守的。L11是大肠杆菌核糖体中甲基化程度最高的蛋白。然而，古细菌L11e蛋白的甲基化位点通常并不保守。L11与古细菌L11e蛋白之间序列相似性最高的区域是N端结构域。该结构域被认为在翻译终止过程中与释放因子1相互作用。将古细菌L1e蛋白的氨基酸序列与真细菌的大肠杆菌L1和嗜热脂肪芽孢杆菌（Bacillus stearothermophilus）L1e序列进行了比较。古细菌L1e蛋白的N端和C端都略短。在蛋白中心附近出现了一个高序列相似性区域（14个残基中有7个）。
