Aloy Patrick, Ciccarelli Francesca D, Leutwein Christina, Gavin Anne-Claude, Superti-Furga Giulio, Bork Peer, Bottcher Bettina, Russell Robert B
EMBL, Meyerhofstrasse, Heidelberg, Germany.
EMBO Rep. 2002 Jul;3(7):628-35. doi: 10.1093/embo-reports/kvf135.
We present a model of the yeast exosome based on the bacterial degradosome component polynucleotide phosphorylase (PNPase). Electron microscopy shows the exosome to resemble PNPase but with key differences likely related to the position of RNA binding domains, and to the location of domains unique to the exosome. We use various techniques to reduce the many possible models of exosome subunits based on PNPase to just one. The model suggests numerous experiments to probe exosome function, particularly with respect to subunits making direct atomic contacts and conserved, possibly functional residues within the predicted central pore of the complex.
我们提出了一种基于细菌降解体成分多核苷酸磷酸化酶（PNPase）的酵母外切体模型。电子显微镜显示，外切体与PNPase相似，但存在一些关键差异，这些差异可能与RNA结合结构域的位置以及外切体特有的结构域位置有关。我们使用各种技术，将基于PNPase的外切体亚基的众多可能模型简化为仅一种。该模型提出了许多用于探究外切体功能的实验，特别是关于在复合物预测的中央孔内进行直接原子接触的亚基以及保守的、可能具有功能的残基的实验。
