DAVID MCKAY PRT TIME

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。子项目和 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。 我们正在继续研究分子伴侣蛋白的结构和机制，广义上说，分子伴侣蛋白有助于细胞中蛋白质和RNA分子的正确折叠、组装和靶向。 目前正在研究的系统包括“原核蛋白酶体”，一种850 kDa的复合物，它是真核蛋白酶体的简单同系物;一种称为通用应激蛋白的“应激耐受”因子家族;一种促进细菌中膜蛋白折叠和组装的伴侣蛋白;以及一种调节细胞中RNA结构的RNA伴侣蛋白/解旋酶家族。 此外，我们正在继续研究小催化RNA或核酶的结构和机制。

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. We are continuing our studies on the structures and mechanisms of molecular chaperone proteins which, broadly speaking, facilitate the correct folding, assembly and targeting of proteins and RNA molecules in cells. Systems that are currently under study include a "prokaryotic proteasome", a 850 kDa complex that is a simple homolog of the eukaryotic proteasome; a family of "stress endurance" factors called universal stress proteins; a chaperone that facilitates folding and assembly of membrane proteins in bacteria; and a family of RNA chaperones/helicases that modulate RNA structure in cells. Additionally, we are continuing our studies on the structure and mechanism of small catalytic RNAs, or ribozymes.