Henderson G, Krygsman P, Liu C J, Davey C C, Malek L T
J Bacteriol. 1987 Aug;169(8):3778-84. doi: 10.1128/jb.169.8.3778-3784.1987.
Protease A and protease B are extracellular proteins which are secreted by Streptomyces griseus. The genes encoding protease A (sprA) and protease B (sprB) were isolated from an S. griseus genomic library by using a synthetic oligonucleotide probe. Fragments containing sprA and sprB were characterized by hybridization and demonstration of proteolytic activity in Streptomyces lividans. Each DNA sequence contains a large open reading frame with the coding region of the mature protease situated at its carboxy terminus. The amino terminus of each reading frame appears to encode a 38-amino-acid signal peptide followed by a 76- or 78-amino-acid polypeptide, a propeptide, which is joined to the mature protease. Strong homology between the coding regions of the protease genes suggests that sprA and sprB originated by gene duplication.
蛋白酶A和蛋白酶B是由灰色链霉菌分泌的细胞外蛋白质。通过使用合成寡核苷酸探针，从灰色链霉菌基因组文库中分离出编码蛋白酶A（sprA）和蛋白酶B（sprB）的基因。含有sprA和sprB的片段通过杂交以及在变铅青链霉菌中蛋白酶活性的证明来进行表征。每个DNA序列都包含一个大的开放阅读框，成熟蛋白酶的编码区位于其羧基末端。每个阅读框的氨基末端似乎编码一个38个氨基酸的信号肽，接着是一个76或78个氨基酸的多肽，即前肽，它与成熟蛋白酶相连。蛋白酶基因编码区之间的高度同源性表明sprA和sprB是通过基因复制产生的。
