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驱动蛋白分子的多功能性基础在于其对鞭毛摆动的调节作用。

Versatile properties of dynein molecules underlying regulation in flagellar oscillation.

机构信息

Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.

Department of Physics, Graduate School of Science, The University of Tokyo, Tokyo, Japan.

出版信息

Sci Rep. 2023 Jun 29;13(1):10514. doi: 10.1038/s41598-023-37242-6.

Abstract

Dynein is a minus-end-directed motor that generates oscillatory motion in eukaryotic flagella. Cyclic beating, which is the most significant feature of a flagellum, occurs by sliding spatiotemporal regulation by dynein along microtubules. To elucidate oscillation generated by dynein in flagellar beating, we examined its mechanochemical properties under three different axonemal dissection stages. By starting from the intact 9 + 2 structure, we reduced the number of interacting doublets and determined three parameters, namely, the duty ratio, dwell time and step size, of the generated oscillatory forces at each stage. Intact dynein molecules in the axoneme, doublet bundle and single doublet were used to measure the force with optical tweezers. The mean forces per dynein determined under three axonemal conditions were smaller than the previously reported stall forces of axonemal dynein; this phenomenon suggests that the duty ratio is lower than previously thought. This possibility was further confirmed by an in vitro motility assay with purified dynein. The dwell time and step size estimated from the measured force were similar. The similarity in these parameters suggests that the essential properties of dynein oscillation are inherent to the molecule and independent of the axonemal architecture, composing the functional basis of flagellar beating.

摘要

动力蛋白是一种负向末端导向的分子马达,能够在真核鞭毛中产生振荡运动。鞭毛的最显著特征是周期性的摆动,这是通过动力蛋白沿着微管进行时空调节的滑动产生的。为了阐明鞭毛摆动中动力蛋白产生的振荡,我们在三个不同的轴丝剖分阶段检查了其机械化学性质。从完整的 9+2 结构开始,我们减少了相互作用的二联体数量,并确定了在每个阶段产生的振荡力的三个参数,即占空比、停留时间和步长。使用光学镊子测量轴丝中单分子动力蛋白的力。在三种轴丝条件下测定的每个动力蛋白的平均力小于先前报道的轴丝动力蛋白的失速力;这一现象表明占空比低于先前的假设。这一可能性通过体外纯化动力蛋白的运动分析进一步得到证实。从测量的力中估计的停留时间和步长相似。这些参数的相似性表明,动力蛋白振荡的基本特性是分子固有的,独立于轴丝结构,构成了鞭毛摆动的功能基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c555/10310797/5b33e3df0f6c/41598_2023_37242_Fig1_HTML.jpg

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