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首页> 外文期刊>Philosophical Transactions of the Royal Society of London, Series B. Biological Sciences >Chaperones: Needed for both the good times and the bad times
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Chaperones: Needed for both the good times and the bad times

机译：伴侣：好时与坏时都需要

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摘要

In this issue, we explore the assembly roles of protein chaperones, mainly through the portal of their associated human diseases (e.g. cardiomyopathy, cataract, neurodegeneration, cancer and neuropathy). There is a diversity to chaperone function that goes beyond the current emphasis in the scientific literature on their undoubted roles in protein folding and refolding. The focus on chaperone-mediated protein folding needs to be broadened by the original Laskey discovery that a chaperone assists the assembly of an oligomeric structure, the nucleosome, and the subsequent suggestion by Ellis that other chaperones may function in assembly processes, as well as in folding. There have been a number of recent discoveries that extend this relatively neglected aspect of chaperone biology to include proteostasis, maintenance of the cellular redox potential, genome stability, transcriptional regulation and cytoskeletal dynamics. So central are these processes that we propose that chaperones stand at the crossroads of life and death because they mediate essential functions, not only during the bad times, but also in the good times. We suggest that chaperones facilitate the success of a species, and hence the evolution of individuals within populations, because of their contributions to so many key cellular processes, of which protein folding is only one.
机译：在本期中，我们主要通过蛋白伴侣的相关人类疾病（例如心肌病，白内障，神经退行性疾病，癌症和神经病）的门户网站探索蛋白伴侣的组装作用。伴侣蛋白功能的多样性超出了科学文献中当前对其在蛋白质折叠和再折叠中的无疑作用的重视。最初的Laskey发现，伴侣可以协助寡聚结构，核小体的组装，随后Ellis提出其他伴侣可以在组装过程中发挥作用，因此，人们需要扩大对伴侣蛋白介导的蛋白质折叠的关注。折叠。最近有许多发现将伴侣生物学的这一相对被忽视的方面扩展到包括蛋白稳态，维持细胞氧化还原电位，基因组稳定性，转录调控和细胞骨架动力学。这些过程至关重要，我们建议伴侣分子站在生与死的十字路口，因为它们不仅在困难时期而且在繁荣时期都发挥着重要作用。我们建议伴侣分子促进一个物种的成功，并因此促进种群内个体的进化，因为它们对许多关键细胞过程的贡献，而蛋白质折叠只是其中的一个。

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