Baardsnes J, Sidhu S, MacLeod A, Elliott J, Morden D, Watson J, Borgford T
Department of Chemistry, Simon Fraser University, Burnaby, British Columbia, Canada.
J Bacteriol. 1998 Jun;180(12):3241-4. doi: 10.1128/JB.180.12.3241-3244.1998.
Streptomyces griseus protease B, a member of the chymotrypsin superfamily, is encoded by a gene that express a pre-pro-mature protein. During secretion the precursor protein is processed into a mature, fully folded protease. In this study, we constructed a family of genes which encode deletions at the amino-terminal end of the propeptide. The secretion of active protease B was seen to decrease in an exponential manner according to the length of the deletion. The results underscore the intimate relationship between folding and secretion in bacterial protease expression. They further suggest that the propeptide segment of the zymogen stabilizes the folding of the mature through many small binding interactions over the entire surface of the peptide rather than through a few specific contacts.
灰色链霉菌蛋白酶B是胰凝乳蛋白酶超家族的成员，由一个表达前原成熟蛋白的基因编码。在分泌过程中，前体蛋白被加工成成熟的、完全折叠的蛋白酶。在本研究中，我们构建了一系列编码前肽氨基末端缺失的基因。根据缺失长度，活性蛋白酶B的分泌呈指数下降。这些结果强调了细菌蛋白酶表达中折叠与分泌之间的密切关系。它们进一步表明，酶原的前肽片段通过在肽的整个表面上的许多小结合相互作用来稳定成熟蛋白的折叠，而不是通过少数特定的接触。
