YEAST KEX2 PROTEASE AND MANNOSYLTRANSFERASE-I ARE LOCALIZED TO DISTINCT COMPARTMENTS OF THE SECRETORY PATHWAY
YEAST KEX2 PROTEASE AND MANNOSYLTRANSFERASE-I ARE LOCALIZED TO DISTINCT COMPARTMENTS OF THE SECRETORY PATHWAY
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DOI：
10.1002/yea.320050105
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发表时间：
1989-01-01
期刊：
影响因子：
2.6
通讯作者：
WICKNER, WT
中科院分区：
文献类型：
--
作者：
CUNNINGHAM, KW;WICKNER, WT
KEX2蛋白酶(KEX2基因的产物)通过在配对的碱性氨基酸残基处切割前杀伤毒素前体和前α因子前体的多肽链，在酿酒酵母的分泌途径中发挥作用。含有 KEX2 蛋白酶的细胞内囊泡以密度梯度沉积到与含有甘露糖基转移酶 I（MNN1 gne 的产物）（高尔基复合体的标记酶）的囊泡不同的位置。沉淀后含有这些酶的完整区室的回收率接近 80%。我们认为 KEX2 蛋白酶和甘露糖基转移酶 I 位于不同的区室中。
The KEX2 protease (product of the KEX2 gene) functions late in the secretory pathway of Saccharomyces cerevisiae by cleaving the polypeptide chains of prepro-killer toxin and prepro-.alpha.-factor at paired basic amino acid residues. The intracellular vesicles containing KEX2 protease sedimented in density gradients to a position distinct from those containing mannosyltransferase I (product of the MNN1 gne), a marker enzyme for the Golgi complex. The recovery of intact compartments containing these enzymes approached 80% after sedimentation. We propose that the KEX2 protease and mannosyltransferase I reside within distinct compartments.