Schlumpberger M, Schaeffeler E, Straub M, Bredschneider M, Wolf D H, Thumm M
Institut für Biochemie, Universität Stuttgart, Germany.
J Bacteriol. 1997 Feb;179(4):1068-76. doi: 10.1128/jb.179.4.1068-1076.1997.
Autophagocytosis is a starvation-induced process responsible for transport of cytoplasmic proteins to the vacuole. In Saccharomyces cerevisiae, autophagy is characterized by the phenotypic appearance of autophagic vesicles inside the vacuole of strains deficient in proteinase yscB. The AUT1 gene, essential for autophagy, was isolated by complementation of the sporulation deficiency of a diploid aut1-1 mutant strain by a yeast genomic library and characterized. AUT1 is located on the right arm of chromosome XIV, 10 kb from the centromere, and encodes a protein of 310 amino acids, with an estimated molecular weight of 36 kDa. Cells carrying a chromosomal deletion of AUT1 are defective in the starvation-induced bulk flow transport of cytoplasmic proteins to the vacuole. aut1 null mutant strains are completely viable but show decreased survival rates during starvation. Homozygous delta aut1 diploid cells fail to sporulate. The selective cytoplasm-to-vacuole transport of aminopeptidase I is blocked in logarithmically growing and in starved delta autl cells. Deletion of the AUT1 gene had no obvious influence on secretion, fluid phase endocytosis, or vacuolar protein sorting. This supports the idea of autophagocytosis as being a novel route transporting proteins from the cytoplasm to the vacuole.
自噬作用是一种由饥饿诱导的过程,负责将细胞质蛋白转运至液泡。在酿酒酵母中,自噬的特征是在蛋白酶yscB缺陷菌株的液泡内出现自噬小泡的表型。通过用酵母基因组文库互补二倍体aut1-1突变菌株的孢子形成缺陷,分离并鉴定了对自噬至关重要的AUT1基因。AUT1位于第十四号染色体的右臂,距着丝粒10 kb,编码一个由310个氨基酸组成的蛋白质,估计分子量为36 kDa。携带AUT1染色体缺失的细胞在饥饿诱导的细胞质蛋白向液泡的大量流动运输中存在缺陷。aut1缺失突变菌株完全可以存活,但在饥饿期间存活率降低。纯合的δaut1二倍体细胞无法形成孢子。在对数生长期和饥饿的δautl细胞中,氨肽酶I的选择性细胞质到液泡运输被阻断。AUT1基因的缺失对分泌、液相内吞作用或液泡蛋白分选没有明显影响。这支持了自噬作用是一种将蛋白质从细胞质转运至液泡的新途径的观点。