Analysis of the of the interaction between the SecY protein translocation complex and its substrate pre-protein

SecY蛋白易位复合物与其底物前蛋白相互作用分析

基本信息

批准号：
BB/F007248/1
负责人：
Ian Collinson
金额：
$ 39.82万
依托单位：
University of Bristol
依托单位国家：
英国
项目类别：
Research Grant
财政年份：
2007
资助国家：
英国
起止时间：
2007 至无数据
项目状态：
已结题

来源：
https://gtr.ukri.org/projects?ref=BB%2FF007248%2F1
关键词：
Analysis interaction between SecY protein

项目摘要

An ancient and essential development for life on Earth has been the evolution of a thin film of lipids that surround and form each cell. These membranes provide a barrier to water and hydrophilic solutes. They serve to isolate biological reactions from the outside, and offer the potential to separate charge and to communicate and combine with one another to form complex structures. More complicated cells also contain internal membrane structures that provide a further division for chemical reactions and generation of electric potentials. These events facilitated the ability to harness energy and to develop and maintain the complex structures and biochemistry of the cell. The necessary exchange of materials across lipid membranes between the outside and different compartments gives rise to a transport problem for small and large molecules alike. Proteins are large polymers of amino acids made according to the genetic code of each respective gene in the cell cytosol. In order to perform their specific roles many of them need to be specifically targeted and delivered to alternative locations. This requires that they pass either across or into a specific membrane. This proposal aims to learn more about this important process using the bacterial cell membrane as a model system. The apparatus responsible for protein movement across membranes has been purified. The interaction of this protein channel and its polypeptide substrate will be studies using a variety of biochemical and biophysical approaches that we have at our disposal. New findings in this area will have implications in the understanding of protein translocation. Moreover, they will also help us understand numerous other important problems in biology that involve the interaction of protein complexes with polypeptides.

地球上生命的古老而基本的发展是围绕和形成每个细胞的脂质薄膜的演变。这些膜为水和亲水溶质提供了障碍。它们有助于将生物反应与外部分离，并提供分离电荷并彼此结合以形成复杂结构的潜力。更复杂的细胞还包含内部膜结构，为化学反应和电势的产生提供了进一步的分裂。这些事件促进了利用能量，开发和维持细胞的复杂结构和生物化学的能力。在外部和不同隔室之间跨脂质膜的材料的必要交换导致大小分子的运输问题。蛋白质是根据细胞胞质中每个基因的遗传密码制成的氨基酸的大聚合物。为了履行其特定角色，其中许多需要专门定位并将其交付到替代位置。这要求它们将它们跨过或进入特定的膜。该建议旨在使用细菌细胞膜作为模型系统了解有关此重要过程的更多信息。负责跨膜蛋白质运动的设备已纯化。该蛋白质通道及其多肽底物的相互作用将使用我们可以使用的多种生化和生物物理方法进行研究。该领域的新发现将对蛋白质易位的理解有影响。此外，它们还将帮助我们了解生物学中许多其他重要问题，这些问题涉及蛋白质复合物与多肽的相互作用。

项目成果

期刊论文数量（5）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Structure of the SecY complex unlocked by a preprotein mimic.

DOI：
10.1016/j.celrep.2011.11.003
发表时间：
2012-01-26
期刊：
Cell reports
影响因子：
8.8
作者：
Hizlan D;Robson A;Whitehouse S;Gold VA;Vonck J;Mills D;Kühlbrandt W;Collinson I
通讯作者：
Collinson I

Dynamic nuclear polarization-enhanced solid-state NMR of a 13C-labeled signal peptide bound to lipid-reconstituted Sec translocon.

与脂质重构的 Sec 易位子结合的 13C 标记信号肽的动态核极化增强固态 NMR。