Department of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 36006, Israel.
FEBS Lett. 2013 Mar 1;587(5):389-93. doi: 10.1016/j.febslet.2013.01.014. Epub 2013 Jan 17.
The 26S proteasome is thought to be a homogenous complex, consisting of a 20S proteolytic core and a 19S regulatory particle that is required for its activation. Two groups have recently reported the activation of archeal 20S by a p97-related double-ring AAA+ ATPase complex, in a similar fashion to that reported for 19S. Since p97 is found in eukaryotes, the existence of a parallel setting in higher organisms is intriguing. Herein, we present supporting data and hypothesize that in eukaryotes, p97 and CSN form a promiscuous, hence hard-to-detect, "alternative cap", enabling the prompt and precise elimination of particular substrates.
26S 蛋白酶体被认为是一种同质复合物，由一个 20S 蛋白水解核心和一个 19S 调节颗粒组成，后者对于其激活是必需的。最近有两个小组报道了 p97 相关的双环 AAA+ATP 酶复合物对古菌 20S 的激活，其方式与报道的 19S 类似。由于 p97 存在于真核生物中，因此在高等生物中存在平行的设置是很有趣的。在这里，我们提供了支持性数据，并假设在真核生物中，p97 和 CSN 形成了一种混杂的、因此难以检测到的“替代帽”，从而能够快速而精确地消除特定的底物。
