Davidow L S, O'Donnell M M, Kaczmarek F S, Pereira D A, DeZeeuw J R, Franke A E
Pfizer Central Research, Groton, Connecticut 06340.
J Bacteriol. 1987 Oct;169(10):4621-9. doi: 10.1128/jb.169.10.4621-4629.1987.
The XPR2 gene encoding an alkaline extracellular protease (AEP) from Yarrowia lipolytica was cloned, and its complete nucleotide sequence was determined. The amino acid sequence deduced from the nucleotide sequence reveals that the mature AEP consists of 297 amino acids with a relative molecular weight of 30,559. The gene codes for a putative 22-amino-acid prepeptide (signal sequence) followed by an additional 135-amino-acid propeptide containing a possible N-linked glycosylation site and two Lys-Arg peptidase-processing sites. The final Lys-Arg site occurs at the junction with the mature, extracellular form. The mature protease contains two potential glycosylation sites. AEP is a member of the subtilisin family of serine proteases, with 42.6% homology to the fungal proteinase K. The functional promoter is more than 700 base pairs long, allowing for the observed complex regulation of this gene. The 5' and 3' flanking regions of the XPR2 gene have structural features in common with other yeast genes.
克隆了编码解脂耶氏酵母碱性细胞外蛋白酶（AEP）的XPR2基因，并测定了其完整的核苷酸序列。从核苷酸序列推导的氨基酸序列表明，成熟的AEP由297个氨基酸组成，相对分子质量为30,559。该基因编码一个推定的22个氨基酸的前肽（信号序列），其后是一个额外的135个氨基酸的前肽，其中包含一个可能的N-连接糖基化位点和两个赖氨酸-精氨酸肽酶加工位点。最后的赖氨酸-精氨酸位点位于与成熟的细胞外形式的交界处。成熟的蛋白酶含有两个潜在的糖基化位点。AEP是丝氨酸蛋白酶枯草杆菌蛋白酶家族的成员，与真菌蛋白酶K有42.6%的同源性。功能性启动子长度超过700个碱基对，允许对该基因进行观察到的复杂调控。XPR2基因的5'和3'侧翼区域具有与其他酵母基因共同的结构特征。
