Bardy Sonia L, Eichler Jerry, Jarrell Ken F
Department of Microbiology and Immunology, Queen's University, Kingston, ON Canada K7L 3N6.
Protein Sci. 2003 Sep;12(9):1833-43. doi: 10.1110/ps.03148703.
The correct delivery of noncytoplasmic proteins to locations both within and outside the cell depends on the appropriate targeting signals. Protein translocation across the bacterial plasma membrane and the eukaryal endoplasmic reticulum membrane relies on cleavable N-terminal signal peptides. Although the signal peptides of secreted proteins in Bacteria and Eukarya have been extensively studied at the sequence, structure, and functional levels, little is known of the nature of archaeal signal peptides. In this report, genome-based analysis was performed in an attempt to define the amino acid composition, length, and cleavage sites of various signal peptide classes in a wide range of archaeal species. The results serve to present a picture of the archaeal signal peptide, revealing the incorporation of bacterial, eukaryal, and archaeal traits.
非细胞质蛋白正确转运至细胞内和细胞外的特定位置取决于适当的靶向信号。蛋白质穿过细菌质膜和真核生物内质网膜的转运依赖于可裂解的N端信号肽。尽管细菌和真核生物中分泌蛋白的信号肽已在序列、结构和功能水平上得到广泛研究，但对于古菌信号肽的性质却知之甚少。在本报告中，我们进行了基于基因组的分析，试图确定广泛的古菌物种中各种信号肽类别的氨基酸组成、长度和切割位点。研究结果描绘了古菌信号肽的情况，揭示了细菌、真核生物和古菌特征的融合。
