内向整流 K+ 通道对双分子层特性的协调是一个由蛋白质-脂质相互作用驱动的合作过程

IF 3.5 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Evan J. van Aalst , Maryam Yekefallah , Roy A. M. van Beekveld , Eefjan Breukink , Markus Weingarth , Benjamin J. Wylie
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引用次数: 0

摘要

生物膜的物理特性直接或间接地影响着生物过程。然而,由于膜蛋白、单个脂质和膜结构之间存在相互影响,因此很难评估膜蛋白和完整膜蛋白之间的相互作用。我们之前利用固态核磁共振(SSNMR)研究发现,细菌内向整流 K+ 通道 KirBac1.1 通过拴系阴离子脂质而核化双分子层有序化和微域的形成。相反,这些脂质与阳离子残基合作结合,激活通道并启动 K+ 通量。然而,控制脂质合作负载与双分子层有序化之间关系的机制细节尚不清楚。为了进行研究,我们生成了含有不同浓度 13C 锂化磷脂酰甘油 (PG) 脂质的 KirBac1.1 样品,并使用有序的全反式 (AT) 和无序的反式-高切 (TG)酰构象作为双分子层动态的标记,获得了一整套 SSNMR 1D 温度序列实验。我们观察到随着 PG 浓度的增加,AT 有序信号增加,TG 无序信号减少,双分子层熔融温度升高。此外,我们还发现了有序化与 PG 脂类直接结合之间的合作关系,这表明 KirBac1.1 驱动的双分子层有序化和微域形成是一个经典的合作希尔型过程,由 PG 脂类直接结合驱动并以其为前提。我们的研究结果为蛋白质和脂质如何共同促成脂膜超分子双分子层异质性提供了独特的机理见解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Coordination of bilayer properties by an inward-rectifier K+ channel is a cooperative process driven by protein-lipid interaction

Coordination of bilayer properties by an inward-rectifier K+ channel is a cooperative process driven by protein-lipid interaction

Physical properties of biological membranes directly or indirectly govern biological processes. Yet, the interplay between membrane and integral membrane proteins is difficult to assess due to reciprocal effects between membrane proteins, individual lipids, and membrane architecture. Using solid-state NMR (SSNMR) we previously showed that KirBac1.1, a bacterial Inward-Rectifier K+ channel, nucleates bilayer ordering and microdomain formation through tethering anionic lipids. Conversely, these lipids cooperatively bind cationic residues to activate the channel and initiate K+ flux. The mechanistic details governing the relationship between cooperative lipid loading and bilayer ordering are, however, unknown. To investigate, we generated KirBac1.1 samples with different concentrations of 13C-lableded phosphatidyl glycerol (PG) lipids and acquired a full suite of SSNMR 1D temperature series experiments using the ordered all-trans (AT) and disordered trans-gauche (TG) acyl conformations as markers of bilayer dynamics. We observed increased AT ordered signal, decreased TG disordered signal, and increased bilayer melting temperature with increased PG concentration. Further, we identified cooperativity between ordering and direct binding of PG lipids, indicating KirBac1.1-driven bilayer ordering and microdomain formation is a classically cooperative Hill-type process driven by and predicated upon direct binding of PG lipids. Our results provide unique mechanistic insight into how proteins and lipids in tandem contribute to supramolecular bilayer heterogeneity in the lipid membrane.

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来源期刊
Journal of Structural Biology: X
Journal of Structural Biology: X Biochemistry, Genetics and Molecular Biology-Structural Biology
CiteScore
6.50
自引率
0.00%
发文量
20
审稿时长
62 days
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