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首页> 外文期刊>Molecular and Cellular Biology >Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles.
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Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles.

机译：酿酒酵母ATX2抑制氧化损伤，该毒素编码定位在高尔基样小泡中的贩运锰的蛋白质。

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Oxygen toxicity in Saccharomyces cerevisiae lacking the copper/zinc superoxide dismutase (SOD1) can be suppressed by overexpression of the S. cerevisiae ATX2 gene. Multiple copies of ATX2 were found to reverse the aerobic auxotrophies of sod1(delta) mutants for lysine and methionine and also to enhance the resistance of these yeast strains to paraquat and atmospheric levels of oxygen. ATX2 encodes a novel 34.4-kDa polypeptide with a number of potential membrane-spanning domains. Our studies indicate that Atx2p localizes to the membrane of a vesicular compartment in yeast cells reminiscent of the Golgi apparatus. With indirect immunofluorescence microscopy, Atx2p exhibited a punctate pattern of staining typical of the Golgi apparatus, and upon subcellular fractionation, Atx2p colocalized with a biochemical marker for the yeast Golgi apparatus. We demonstrate here that this vesicle protein normally functions in the homeostasis of manganese ions and that this role in metal metabolism is necessary for the ATX1 suppression of SOD1 deficiency. First, overexpression of ATX2 caused cells to accumulate increased levels of manganese. Second, a deletion in ATX2 caused a decrease in the apparent available level of intracellular manganese and caused sod1(delta) mutants to become dependent upon exogenous manganese for aerobic growth. Third, ATX2 was incapable of suppressing oxidative damage in cells depleted of manganese ions or lacking the plasma membrane transporter for manganese. The effect of ATX2 overexpression on manganese accumulation and oxygen resistance is similar to what we have previously reported for mutations in PMR1, which encodes a manganese-trafficking protein that also resides in a vesicular compartment. Our studies are consistent with a model in which Atx2p and Pmr1p work in opposite directions to control manganese homeostasis.
机译：酿酒酵母中缺乏铜/锌超氧化物歧化酶（SOD1）的氧中毒可通过酿酒酵母ATX2基因的过表达来抑制。发现ATX2的多个副本可以逆转sod1（delta）突变体的赖氨酸和蛋氨酸的有氧营养缺陷型，还可以增强这些酵母菌株对百草枯和大气中氧气的抵抗力。 ATX2编码具有许多潜在跨膜结构域的新型34.4-kDa多肽。我们的研究表明，Atx2p定位于让人联想到高尔基体的酵母细胞的囊泡室膜上。用间接免疫荧光显微镜观察，Atx2p表现出点状的高尔基体染色特征，亚细胞分级分离后，Atx2p与酵母高尔基体的生化标记共定位。我们在这里证明了这种囊泡蛋白通常在锰离子的体内平衡中起作用，并且在金属代谢中的这种作用对于ATX1抑制SOD1缺乏是必需的。首先，ATX2的过表达导致细胞积累锰水平升高。其次，ATX2的缺失导致细胞内锰的表观可用水平降低，并导致sod1（delta）突变体变得依赖于外源锰的有氧生长。第三，ATX2不能抑制贫锰离子或缺乏锰质膜转运蛋白的细胞的氧化损伤。 ATX2过表达对锰积累和抗氧性的影响与我们先前报道的PMR1突变相似，后者编码一种锰转运蛋白，该蛋白也存在于囊泡区。我们的研究与其中Atx2p和Pmr1p在相反方向上控制锰稳态的模型是一致的。

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