Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome.
Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome.
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pep7 突变与 PEP12 和 VPS45 基因之间的遗传相互作用：酿酒酵母高尔基体复合体和内体之间运输中新的 SNARE 成分的证据。
DOI：
10.1093/genetics/147.2.467
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发表时间：
1997
期刊：
影响因子：
3.3
通讯作者：
Jones,EW
中科院分区：
文献类型：
--
作者：
Webb,GC;Hoedt,M;Poole,LJ;Jones,EW
酵母PEP 7基因编码一个59 kD的亲水性多肽，该多肽是将可溶性液泡水解酶前体从TGN转运到内体所必需的。本研究提供了pep 7 - 20突变表型的高拷贝抑制分析结果。该分析表明VPS 45和PEP 12都是pep 7 - 20突变表型的等位基因特异性高拷贝抑制子。VPS 45的过表达能够完全抑制Zn ~（2+）敏感性，部分抑制羧肽酶Y缺乏。PEP 12的过表达也能做到这一点，但程度较低。Vps 45 p和Pep 12 p分别是Sec 1 p和突触融合蛋白（t-SNARE）的同源物，也被认为在TGN和内体之间的转运中起作用。另外两个空泡途径SNARE复合物同源物，Vps 33 p（Sec 1 p）和Pth 1 p（syntaxin），当过表达时，不能抑制pep 7 - 20或任何其他pep 7等位基因，进一步支持pep 7 - 20与PEP 12和VPS 45相互作用的特异性。由于其他几个囊泡对接/融合反应发生在细胞中没有明显的参与Pep 7 p同源物，我们建议，Pep 7 p是一个步骤特定的调节剂的对接和/或融合TGN衍生的运输囊泡到内体。
ThePEP7gene fromSaccharomyces cerevisiaeencodes a 59-kD hydrophilic polypeptide that is required for transport of soluble vacuolar hydrolase precursors from the TGN to the endosome. This study presents the results of a high-copy suppression analysis ofpep7-20mutant phenotypes. This analysis demonstrated that bothVPS45andPEP12are allele-specific high-copy suppressors ofpep7-20mutant phenotypes. Overexpression ofVPS45was able to completely suppress the Zn2+sensitivity and partially suppress the carboxypeptidase Y deficiency. Overexpression ofPEP12was able to do the same, but to a lesser extent. Vps45p and Pep12p are Sec1p and syntaxin (t-SNARE) homologues, respectively, and are also thought to function in transport between the TGN and endosome. Two additional vacuole pathway SNARE complex homologues, Vps33p (Sec1p) and Pth1p (syntaxin), when overexpressed, were unable to suppresspep7-20or any otherpep7allele, further supporting the specificity of the interactions ofpep7-20withPEP12andVPS45. Because several other vesicle docking/fusion reactions take place in the cell without discernible participation of Pep7p homologues, we suggest that Pep7p is a step-specific regulator of docking and/or fusion of TGN-derived transport vesicles onto the endosome.