Archaea are a valuable source of enzymes for industrial and scientific applications because of their ability to survive extreme conditions including high salt and temperature. Thanks to advances in molecular biology and genetics, archaea are also attractive hosts for metabolic engineering. Understanding how energy-dependent proteases and chaperones function to maintain protein quality control is key to high-level synthesis of recombinant products. In archaea, proteasomes are central players in energy-dependent proteolysis and form elaborate nanocompartments that degrade proteins into oligopeptides by processive hydrolysis. The catalytic core responsible for this proteolytic activity is the 20S proteasome, a barrel-shaped particle with a central channel and axial gates on each end that limit substrate access to a central proteolytic chamber. AAA proteins (ATPases associated with various cellular activities) are likely to play several roles in mediating energy-dependent proteolysis by the proteasome. These include ATP binding/hydrolysis, substrate binding/unfolding, opening of the axial gates, and translocation of substrate into the proteolytic chamber.

中文翻译：

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古细菌蛋白酶体：在代谢工程中的潜力。

古细菌是工业和科学应用中酶的重要来源，因为它们能够在包括高盐和高温在内的极端条件下生存。由于分子生物学和遗传学的进步，古细菌也是代谢工程的诱人宿主。了解能量依赖性蛋白酶和伴侣蛋白如何维持蛋白质质量控​​制是重组产物高水平合成的关键。在古细菌中，蛋白酶体是能量依赖性蛋白水解的主要参与者，并形成复杂的纳米隔室，该纳米隔室通过进行性水解将蛋白质降解为寡肽。负责这种蛋白水解活性的催化核心是20S蛋白酶体，它是一种桶形颗粒，具有中央通道和两端的轴向门，限制了底物进入中央蛋白水解室。AAA蛋白（与各种细胞活动相关的ATPase）可能在蛋白酶体介导的能量依赖性蛋白水解中起多种作用。这些包括ATP结合/水解，底物结合/展开，轴向门的打开以及底物向蛋白水解室的转移。