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首页> 外文期刊>The Journal of Experimental Biology >Temperature interactions of the molecular chaperone Hsc70 from theeurythermal marine goby Gillichthys mirabilis
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Temperature interactions of the molecular chaperone Hsc70 from theeurythermal marine goby Gillichthys mirabilis

机译：海洋热虾虎鱼Gillichthys mirabilis分子伴侣Hsc70的温度相互作用

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Molecular chaperones participate in many aspects of protein biogenesis. Mechanistically, they recognize and bind to non-native proteins, prevent the aggregation of unfolded proteins and also, in some cases, facilitate refolding. Although a great deal is known about the cellular function of molecular chaperones in general, very little is known about the effect of temperature on molecular chaperones in non-model organisms, particularly in ectotherms that fold proteins under variable-temperature conditions in nature. To address this issue, we studied the temperature interactions of a major cytosolic molecular chaperone, Hsc70, from the eurythermal marine goby Gillichthys mirabilis. Using in vitro assays, we measured the intrinsic activity, unfolded-protein-stimulated activity, temperature sensitivity and heat stability of the ATPase activity of native Hsc70 purified from G. mirabilis white muscle. Similar to other chaperones in the 70 kDa heat-shock protein family, G. mirabilis Hsc70 exhibited a low intrinsic ATPase activity that was stimulated in vitro by the addition of unfolded protein. Across the environmentally relevant temperature range (10-35 degreesC), the ATPase activity of G. mirabilis Hsc70 displayed differential thermal sensitivity, with the greatest sensitivity occurring between 10 and 15 degreesC and the least sensitivity between 15 and 25 degreesC. In addition, the activity of Hsc70 was not significantly different between the unstimulated and unfolded-protein-stimulated treatments, suggesting that the ATPase activity and the peptide-binding domain of Hsc70 have similar thermal sensitivities in vitro. Finally, the thermal stability of Hsc70 ATPase activity greatly exceeded environmental temperatures for G. mirabilis, with activity up to 62.5 degreesC. Overall, the biochemical characterization of the ATPase activity suggests that, although Hsc70 is not an extraordinarily thermally stable protein, it is capable of protein chaperoning cycles even at the extremes of environmental temperatures encountered by G. mirabilis in nature.
机译：分子伴侣参与蛋白质生物发生的许多方面。从机制上讲，它们识别并结合非天然蛋白质，防止未折叠蛋白质聚集，并且在某些情况下还有助于重新折叠。尽管通常对分子伴侣的细胞功能了解很多，但对温度对非模型生物中分子伴侣的影响知之甚少，特别是在自然界中在可变温度条件下折叠蛋白质的等温线中。为了解决这个问题，我们研究了来自热源海洋虾虎鱼Gillichthys mirabilis的主要胞质分子伴侣Hsc70的温度相互作用。使用体外测定，我们测量了从狂犬病菌白肌肉中纯化的天然Hsc70的内在活性，未折叠蛋白刺激的活性，温度敏感性和ATPase活性的热稳定性。与70 kDa热休克蛋白家族中的其他伴侣相似，奇异芽孢杆菌Hsc70表现出较低的固有ATPase活性，在体外可通过添加未折叠的蛋白来刺激。在与环境有关的温度范围（10-35摄氏度）中，奇异芽孢杆菌Hsc70的ATPase活性表现出不同的热敏感性，最大敏感性出现在10至15摄氏度之间，最小敏感性发生在15至25摄氏度之间。另外，在未刺激和未折叠的蛋白刺激的处理之间，Hsc70的活性没有显着差异，这表明Hsc70的ATP酶活性和肽结合域在体外具有相似的热敏性。最终，Hsc70 ATPase活性的热稳定性大大超出了环境，达到了62.5摄氏度。总体而言，ATPase活性的生化特征表明，尽管Hsc70不是异常热稳定的蛋白质，但即使在自然条件下出现的极端微生物（极端情况下），它也能够进行蛋白伴侣循环。

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