DETERMINING THE PATHWAY OF NASCENT-PROTEIN INSERTION THROUGH THE PROTEIN-CONDUC

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 对于要排泄或膜插入的新生蛋白质，核糖体的合成伴随着它们插入到蛋白质传导膜通道SecY中，该通道将蛋白质转移到膜上或将其插入膜中。在与冷冻电子显微镜的合作下，我们确定了核糖体-SecY-新生蛋白中间体的全原子结构，使人们能够研究膜插入途径。我们试图模拟我们结构的膜-SecY-新生蛋白质部分，以确定揭示的中间产物，即在SecY侧门外定向倒置的N-末端结合，是如何由蛋白质伸长引起的力产生的。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. For nascent proteins destined for excretion or membrane insertion, synthesis by the ribosome is concomitant with their insertion into a protein-conducting membrane channel, SecY, which translocates a protein across or inserts it into the membrane. In collaboration with cryo-electron microscopists we determined an all-atom structure of a ribosome-SecY-nascent-protein intermediate that permits one to investigate the membrane insertion pathway. We seek to simulate the membrane-SecY-nascent protein part of our structure to determine how the intermediate revealed, an orientationally inverted N-terminus binding outside a SecY lateral gate, arises from forces due to protein elongation.