van Wely K H, Swaving J, Broekhuizen C P, Rose M, Quax W J, Driessen A J
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9751 NN Haren, The Netherlands.
J Bacteriol. 1999 Mar;181(6):1786-92. doi: 10.1128/JB.181.6.1786-1792.1999.
Protein export in Escherichia coli is mediated by translocase, a multisubunit membrane protein complex with SecA as the peripheral subunit and the SecY, SecE, and SecG proteins as the integral membrane domain. In the gram-positive bacterium Bacillus subtilis, SecA, SecY, and SecE have been identified through genetic analysis. Sequence comparison of the Bacillus chromosome identified a potential homologue of SecG, termed YvaL. A chromosomal disruption of the yvaL gene results in mild cold sensitivity and causes a beta-lactamase secretion defect. The cold sensitivity is exacerbated by overexpression of the secretory protein alpha-amylase, whereas growth and beta-lactamase secretion are restored by coexpression of yvaL or the E. coli secG gene. These results indicate that the yvaL gene codes for a protein that is functionally homologous to SecG.
大肠杆菌中的蛋白质输出由转位酶介导,转位酶是一种多亚基膜蛋白复合物,其外周亚基为SecA,完整膜结构域为SecY、SecE和SecG蛋白。在革兰氏阳性菌枯草芽孢杆菌中,通过遗传分析已鉴定出SecA、SecY和SecE。对枯草芽孢杆菌染色体的序列比较鉴定出一个潜在的SecG同源物,称为YvaL。yvaL基因的染色体破坏导致轻度冷敏感性,并引起β-内酰胺酶分泌缺陷。分泌蛋白α-淀粉酶的过表达会加剧冷敏感性,而yvaL或大肠杆菌secG基因的共表达可恢复生长和β-内酰胺酶分泌。这些结果表明,yvaL基因编码一种在功能上与SecG同源的蛋白质。