首页> 美国卫生研究院文献>Protein Science : A Publication of the Protein Society >Biogenesis quality control and structural dynamics of proteins as explored in living cells via site‐directed photocrosslinking
【2h】

Biogenesis quality control and structural dynamics of proteins as explored in living cells via site‐directed photocrosslinking

机译:通过地点针对光电区探索的蛋白质生物发生质量控制和结构动态

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务,本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文,但由于OA文献来源多样且变更频繁,仍可能出现获取不到、文献不完整或与标题不符等情况,如果获取不到我们将提供退款服务。请知悉。

摘要

Protein biogenesis and quality control are essential to maintaining a functional pool of proteins and involve numerous protein factors that dynamically and transiently interact with each other and with the substrate proteins in living cells. Conventional methods are hardly effective for studying dynamic, transient, and weak protein–protein interactions that occur in cells. Herein, we review how the site‐directed photocrosslinking approach, which relies on the genetic incorporation of a photoreactive unnatural amino acid into a protein of interest at selected individual amino acid residue positions and the covalent trapping of the interacting proteins upon ultraviolent irradiation, has become a highly efficient way to explore the aspects of protein contacts in living cells. For example, in the past decade, this approach has allowed the profiling of the in vivo substrate proteins of chaperones or proteases under both physiologically optimal and stressful (e.g., acidic) conditions, mapping residues located at protein interfaces, identifying new protein factors involved in the biogenesis of membrane proteins, trapping transiently formed protein complexes, and snapshotting different structural states of a protein. We anticipate that the site‐directed photocrosslinking approach will play a fundamental role in dissecting the detailed mechanisms of protein biogenesis, quality control, and dynamics in the future.
机译:蛋白质生物发生和质量控制对于维持官能团的蛋白质是必不可少的,并且涉及许多蛋白质因子,其彼此动态和瞬时相互作用,并在活细胞中含有底物蛋白。常规方法对于研究细胞中发生的动态,瞬时和弱蛋白质 - 蛋白质相互作用几乎没有有效。在此,我们回顾了网站定向的光关方法的方法,这依赖于在选定的单个氨基酸残基位置和在紫外线辐照上相互作用的蛋白质的感兴趣蛋白质中的遗传掺入蛋白质中的蛋白质掺入蛋白质一种高效的方法来探索活细胞中蛋白质接触的方面。例如,在过去的十年中,这种方法允许在生理上最佳和胁迫(例如,酸性)条件下,在蛋白质界面的映射残留物中允许伴侣蛋白或蛋白酶的体内底物蛋白的分析,鉴定涉及的新蛋白因素膜蛋白的生物发生,捕获瞬时形成的蛋白质复合物,并进行蛋白质的不同结构状态。我们预计站点定向的光电区方法将在解除未来蛋白质生物发生,质量控制和动态的详细机制方面发挥基本作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号