Barth H, Meiling-Wesse K, Epple U D, Thumm M
University of Stuttgart, Institute of Biochemistry, Pfaffenwaldring 55, 70569 Stuttgart, Germany.
FEBS Lett. 2001 Nov 9;508(1):23-8. doi: 10.1016/s0014-5793(01)03016-2.
We here report the identification of AUT10 as a novel gene required for both the cytoplasm to vacuole targeting of proaminopeptidase I and starvation-induced autophagy. aut10Delta cells are impaired in maturation of proaminopeptidase I under starvation and non-starvation conditions. A lack of Aut10p causes a defect in autophagy prior to vacuolar uptake of autophagosomes. Homozygous aut10Delta diploids do not sporulate. Vacuolar acidification indicated by accumulation of quinacrine is normal in aut10Delta cells and mature vacuolar proteinases are present. A biologically active Ha-tagged Aut10p, chromosomally expressed from its endogenous promoter, localizes in indirect immunofluorescence microscopy in the cytosol and on granulated structures, which appear clustered around the vacuolar membrane. This localization differs from known autophagy proteins.
我们在此报告，已鉴定出AUT10是一种新基因，它对于氨肽酶I从细胞质到液泡的靶向运输以及饥饿诱导的自噬均是必需的。在饥饿和非饥饿条件下，aut10Δ细胞中氨肽酶I的成熟均受损。缺乏Aut10p会导致自噬体在液泡摄取之前出现缺陷。纯合的aut10Δ二倍体不能形成孢子。在aut10Δ细胞中，由喹吖因积累所表明的液泡酸化是正常的，并且存在成熟的液泡蛋白酶。从其内源启动子进行染色体表达的具有生物活性的Ha标签Aut10p，在间接免疫荧光显微镜下定位于细胞质溶胶和颗粒状结构上，这些结构似乎聚集在液泡膜周围。这种定位与已知的自噬蛋白不同。
