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Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica

机译:酵母解脂耶氏酵母中唯一已知的Hsc70相互作用蛋白CHIP羧基末端的半胱氨酸直向同源物的分子和功能表征

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摘要

The carboxyl terminus of Hsc70-interacting protein (CHIP) is an Hsp70 co-chaperone and a U-box ubiquitin ligase that plays a crucial role in protein quality control in higher eukaryotes. The yeast Yarrowia lipolytica is the only known hemiascomycete where a CHIP ortholog is found. Here, we characterize Y. lipolytica’s CHIP ortholog (Yl.Chn1p) and document its interactions with components of the protein quality control machinery. We show that Yl.Chn1p is non-essential unless Y. lipolytica is severely stressed. We sought for genetic interactions among key components of the Y. lipolytica protein quality control arsenal, including members of the Ssa-family of Hsp70 molecular chaperones, the Yl.Bag1p Hsp70 nucleotide exchange factor, the Yl.Chn1p and Yl.Ufd2p U-box ubiquitin ligases, the Yl.Doa10p and Yl.Hrd1p RING-finger ubiquitin ligases, and the Yl.Hsp104p disaggregating molecular chaperone. Remarkably, no synthetic phenotypes were observed among null alleles of the corresponding genes in most cases, suggesting that overlapping pathways efficiently act to enable Y. lipolytica cells to survive under harsh conditions. Yl.Chn1p interacts with mammalian and Saccharomyces cerevisiae members of the Hsp70 family in vitro, and these interactions are differently regulated by Hsp70 co-chaperones. We demonstrate notably that Yl.Chn1p/Ssa1p interaction is Fes1p-dependent and the formation of an Yl.Chn1p/Ssa1p/Sse1p ternary complex. Finally, we show that, similar to Sse1p, Yl.Chn1p can act as a “holdase” to prevent the aggregation of a heat-denatured protein.Electronic supplementary materialThe online version of this article (doi:10.1007/s12192-011-0302-6) contains supplementary material, which is available to authorized users.
机译:Hsc70相互作用蛋白(CHIP)的羧基末端是Hsp70伴侣蛋白和U-box泛素连接酶,在高级真核生物的蛋白质质量控​​制中起着至关重要的作用。酵母解脂耶氏酵母是已知的唯一发现CHIP直系同源物的半胱氨酸。在这里,我们描述了解脂耶氏酵母的CHIP直系同源物(Yl.Chn1p),并记录了其与蛋白质质量控​​制机制中各成分的相互作用。我们显示,除非严重解脂耶氏酵母,否则Y1.Chn1p是非必需的。我们寻求解脂耶氏酵母蛋白质质量控​​制库的关键组成部分之间的遗传相互作用,包括Hsp70分子伴侣Ssa家族成员,Yl.Bag1p Hsp70核苷酸交换因子,Yl.Chn1p和Yl.Ufd2p U-box泛素连接酶,Y1.Doa10p和Y1.Hrd1p RING手指泛素连接酶和Y1.Hsp104p分解分子伴侣。值得注意的是,在大多数情况下,在相应基因的无效等位基因中未观察到合成表型,这表明重叠途径有效地起作用以使解脂耶氏酵母细胞能够在恶劣条件下存活。 Yl.Chn1p在体外与Hsp70家族的哺乳动物和酿酒酵母成员相互作用,并且这些相互作用受Hsp70伴侣蛋白的调控。我们特别证明了 Yl。 Chn1p / Ssa1p相互作用是Fes1p依赖性的,并且形成了 Yl。 Chn1p / Ssa1p / Sse1p三元复合物。最后,我们证明了与Sse1p类似, Yl。 Chn1p可以充当“保持酶”以防止热变性蛋白质的聚集。电子补充材料本文的在线版本(doi:10.1007) / s12192-011-0302-6)包含补充材料,授权用户可以使用。

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