STRUCTURAL STUDIES OF MTR4

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 这个项目的主要主题是mtr4蛋白，这是一种高度保守的、必不可少的真核蛋白质，在RNA监测和衰退途径中发挥着核心作用。MTR4是一种RNA解旋酶，它与Trf4(RNA聚合酶)和Air2(锌指蛋白)形成复合体，形成TRAMP？很复杂。通过一种未知的机制，这个复合体识别要降解的RNA，用一条短的PolyA尾巴标记它们，然后将它们递送到外体进行胞外降解。为了阐明依赖TRAMP的RNA监视的结构细节，我们正在测定MTR4及其相关复合体的晶体结构。我们目前的MTR4晶体在原始源上的衍射率很低，需要同步辐射来确定结构。

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. The primary subject of this project is the Mtr4 protein, a highly conserved and essential eukaryotic protein that plays a central role in RNA surveillance and decay pathways. Mtr4 is an RNA helicase that acts in complex with Trf4 (an RNA polymerase) and Air2 (a zinc finger protein) to form the ?TRAMP? complex. By an unknown mechanism, this complex identifies RNAs for degradation, tags them with a short poly-A tail, and then delivers them to the exosome for exonucleolytic degradation. In order to elucidate the structural details of TRAMP-dependent RNA surveillance, we are determining crystal structures of Mtr4 and relevant complexes. Our current Mtr4 crystals diffract poorly on a home source, requiring synchrotron radiation for structure determination.