Moehle C M, Tizard R, Lemmon S K, Smart J, Jones E W
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Mol Cell Biol. 1987 Dec;7(12):4390-9. doi: 10.1128/mcb.7.12.4390-4399.1987.
The PRB1 gene of Saccharomyces cerevisiae encodes the vacuolar endoprotease protease B. We have determined the DNA sequence of the PRB1 gene and the amino acid sequence of the amino terminus of mature protease B. The deduced amino acid sequence of this serine protease shares extensive homology with those of subtilisin, proteinase K, and related proteases. The open reading frame of PRB1 consists of 635 codons and, therefore, encodes a very large protein (molecular weight, greater than 69,000) relative to the observed size of mature protease B (molecular weight, 33,000). Examination of the gene sequence, the determined amino-terminal sequence, and empirical molecular weight determinations suggests that the preproenzyme must be processed at both amino and carboxy termini and that asparagine-linked glycosylation occurs at an unusual tripeptide acceptor sequence.
酿酒酵母的PRB1基因编码液泡内蛋白酶B。我们已确定PRB1基因的DNA序列以及成熟蛋白酶B氨基末端的氨基酸序列。这种丝氨酸蛋白酶推导的氨基酸序列与枯草杆菌蛋白酶、蛋白酶K及相关蛋白酶的氨基酸序列有广泛的同源性。PRB1的开放阅读框由635个密码子组成，因此相对于观察到的成熟蛋白酶B的大小（分子量为33,000），它编码一种非常大的蛋白质（分子量大于69,000）。对基因序列、确定的氨基末端序列以及经验性分子量测定的研究表明，前体酶原必须在氨基末端和羧基末端进行加工，并且天冬酰胺连接的糖基化发生在一个不寻常的三肽受体序列处。
