MECHANISM OF GATE-OPENING IN THE 20S PROTEASOME INDUCED BY PROTEASOMAL ATPASES

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目及 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 在所有真核细胞中，26 S蛋白酶体以ATP依赖的方式催化大多数细胞内蛋白质的降解。蛋白酶体由夹在两个19 S调节复合物（RP）之间的20 S蛋白酶核心颗粒（CP）组成。蛋白酶体ATP酶识别降解的靶底物，解折叠球状底物，诱导20 S中的门打开，并促进解折叠底物易位到20 S CP中进行降解。我们采用单粒子冷冻电镜结合其他生物化学方法研究ATP酶诱导20 S CP门开放的机制。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. In all eukaryotic cells, 26S proteasome catalyzes most intracellular protein degradation in an ATP dependent manner. The proteasome is composed of a 20S protease core particle (CP) sandwiched between two 19S regulatory complexes (RP). The proteasomal ATPases recognize the substrates targeted for the degradations, unfold globular substrates, induce gate-opening in the 20S, and facilitate translocation of the unfolded substrate into 20S CP for degradation. We are using single particle cryoEM together with other biochemical methods to study the mechanism of gate-opening in the 20S CP induced by the ATPases.