Suppr超能文献

水通道蛋白的电压门控,离子胁迫时假定的保守安全机制。

Voltage-gating of aquaporins, a putative conserved safety mechanism during ionic stresses.

机构信息

UCA, INRAE, UMR PIAF, Clermont-Ferrand, France.

Structural Motility, Institut Curie, Paris Université Sciences et Lettres, CNRS UMR144, Sorbonne Université, Paris, France.

出版信息

FEBS Lett. 2021 Jan;595(1):41-57. doi: 10.1002/1873-3468.13944. Epub 2020 Oct 17.

Abstract

Aquaporins are transmembrane water channels found in almost every living organism. Numerous studies have brought a good understanding of both water transport through their pores and the regulations taking place at the molecular level, but subtleties remain to be clarified. Recently, a voltage-related gating mechanism involving the conserved arginine of the channel's main constriction was captured for human aquaporins through molecular dynamics studies. With a similar approach, we show that this voltage-gating could be conserved among this family and that the underlying mechanism could explain part of plant AQPs diversity when contextualized to high ionic concentrations provoked by drought. Finally, we identified residues as adaptive traits which constitute good targets for drought resistance plant breeding research.

摘要

水通道蛋白是存在于几乎所有生物体中的跨膜水分子通道。大量研究已经很好地了解了它们的孔隙中的水运输以及分子水平上的调节,但仍有一些细微之处需要澄清。最近,通过分子动力学研究,发现了一种涉及通道主要收缩部位保守精氨酸的与电压相关的门控机制,用于人类水通道蛋白。通过类似的方法,我们表明这种电压门控可以在这个家族中保守存在,并且潜在的机制可以解释部分植物 AQPs 的多样性,当将其置于由干旱引起的高离子浓度的背景下时。最后,我们确定了一些作为适应特征的残基,这些残基是抗旱植物育种研究的良好目标。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验