Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro.
Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro.
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DOI：
10.1038/s41467-021-23412-5
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发表时间：
2021-06-03
影响因子：
16.6
通讯作者：
Dekker C
中科院分区：
文献类型：
--
作者：
Brauns F;Pawlik G;Halatek J;Kerssemakers J;Frey E;Dekker C
Min蛋白的自组织负责大肠杆菌中细胞分裂的空间控制，并且已经在体内和体外进行了研究。有趣的是，在这些环境中观察到的蛋白质模式在定性和定量上都有所不同。这一令人困惑的二分法至今尚未得到解决。使用重建的蛋白质在横向宽微腔室具有良好的控制高度，我们的实验表明，最小蛋白质的动态膜上的关键取决于微腔室的高度，由于批量浓度梯度正交的膜。理论分析表明，在低微室高度的体外模式是由相同的横向振荡模式驱动的极点到极点的振荡在体内。在较大的微室高度，额外的垂直振荡模式设置，标志着过渡到一个定性不同的体外制度。我们的工作揭示了质的不同机制的质量运输，管理Min蛋白质模式不同的散装高度，从而表明，Min模式在细胞中是由一个不同的机制比那些在体外。在体内和体外观察到的Min蛋白质模式的自组织定性和定量不同。在这里，作者在具有良好控制高度的横向宽微室中重构Min蛋白，并表明膜上的Min蛋白动力学关键取决于微室高度。
Self-organisation of Min proteins is responsible for the spatial control of cell division in Escherichia coli, and has been studied both in vivo and in vitro. Intriguingly, the protein patterns observed in these settings differ qualitatively and quantitatively. This puzzling dichotomy has not been resolved to date. Using reconstituted proteins in laterally wide microchambers with a well-controlled height, we experimentally show that the Min protein dynamics on the membrane crucially depend on the micro chamber height due to bulk concentration gradients orthogonal to the membrane. A theoretical analysis shows that in vitro patterns at low microchamber height are driven by the same lateral oscillation mode as pole-to-pole oscillations in vivo. At larger microchamber height, additional vertical oscillation modes set in, marking the transition to a qualitatively different in vitro regime. Our work reveals the qualitatively different mechanisms of mass transport that govern Min protein-patterns for different bulk heights and thus shows that Min patterns in cells are governed by a different mechanism than those in vitro. Self-organisation of Min protein patterns observed in vivo and in vitro differ qualitatively and quantitatively. Here the authors reconstituted Min proteins in laterally wide microchambers with a well-controlled height and show that the Min protein dynamics on the membrane crucially depend on the micro chamber height.