Functional Analysis of Thiol-Disulfide Oxidoreductases in Streptococcus gordonii

戈登链球菌硫醇二硫化物氧化还原酶的功能分析

• 批准号: 183712-2013
• 负责人: Lee, Song
• 金额: $ 2.62万
• 依托单位: Dalhousie University
• 依托单位国家: 加拿大
• 项目类别: Discovery Grants Program - Individual
• 财政年份: 2017
• 资助国家: 加拿大
• 起止时间: 2017-01-01 至 2018-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=629741
• 关键词: Functional; Analysis; Thiol; Disulfide; Oxidoreductases

A disulfide bond is a stable bond formed between two molecules of the amino acid cysteine. The formation of disulfide bonds is critical to the stability of the proteins because they allow the proteins to fold into an active conformation (shape) to carry out proper functions or activities. A disulfide bond is formed through the action of enzymes called thiol-disulfide oxidoreductases. In Gram-negative bacteria, the disulfide formation pathway is well understood. In contrast, very little is known about how disulfide bonds are formed in Gram-positive bacteria. The proposed research is designed to understand how disulfide bonds are formed in Gram-positive bacteria using Streptococcus gordonii as a model bacterium. S. gordonii is a normal bacterium found in the human mouth as part of the dental plaque. Because of the changing environment in the mouth from food consumption, saliva flow, and frequent movement of the mouth, S. gordonii has developed many traits to become a successful organism. These traits include the ability to form thick layer of plaque on teeth and pick up DNA from the environment. Proteins involved in these traits contain disulfide bonds and it is our goals to identify the enzymes responsible for forming disulfide bonds in these proteins. We will use modern molecular and biochemical techniques to dissect the exact mechanisms of how disulfide bonds are formed in S. gordonii. Thus, the research provides understanding to protein folding and function that is fundamental to biological processes in a cell.

二硫键是两个半胱氨酸分子之间形成的稳定键。二硫键的形成对蛋白质的稳定性至关重要，因为它们允许蛋白质折叠成活性构象（形状）以执行适当的功能或活性。二硫键通过称为硫醇-二硫氧化还原酶的酶的作用形成。在革兰氏阴性菌中，二硫化物形成途径是很好理解的。相比之下，很少有人知道二硫键是如何形成的革兰氏阳性细菌。这项研究旨在了解二硫键是如何在革兰氏阳性细菌中形成的，使用Streptococcus gordonii作为模型细菌。S.戈登氏菌是在人类口腔中作为牙菌斑的一部分发现的正常细菌。由于食物的消耗、唾液的流动和口腔的频繁运动等口腔环境的变化，S。戈登氏鱼已经进化出许多特性，成为一种成功的生物。这些特征包括在牙齿上形成厚层牙菌斑的能力，以及从环境中获取DNA的能力。参与这些性状的蛋白质含有二硫键，我们的目标是鉴定负责在这些蛋白质中形成二硫键的酶。我们将使用现代分子和生物化学技术来剖析S中二硫键如何形成的确切机制。gordonii。因此，这项研究提供了对蛋白质折叠和功能的理解，这对细胞中的生物过程至关重要。