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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.

地球上生命的一个古老而重要的发展是围绕并形成每个细胞的脂质薄膜的进化。这些膜提供了对水和亲水性溶质的屏障。它们的作用是将生物反应与外界隔离开来，并提供分离电荷、相互沟通和联合收割机以形成复杂结构的可能性。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进一步的分裂。这些事件促进了利用能量以及发展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穿过脂质膜的物质的必要交换引起了小分子和大分子的运输问题。蛋白质是根据细胞质溶胶中每个相应基因的遗传密码制成的氨基酸的大聚合物。为了发挥其具体作用，其中许多人需要有具体的目标，并被送到其他地点。这需要它们穿过或进入特定的膜。该提案旨在使用细菌细胞膜作为模型系统来更多地了解这一重要过程。负责蛋白质跨膜运动的装置已被纯化。这种蛋白质通道和它的多肽底物的相互作用将使用各种生物化学和生物物理的方法，我们在我们的处置进行研究。这一领域的新发现将对蛋白质易位的理解产生影响。此外，它们还将帮助我们理解生物学中涉及蛋白质复合物与多肽相互作用的许多其他重要问题。

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。