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科学家利用MINFLUX技术剖析了kinesin-1的无障碍行走
作者:小柯机器人 发布时间:2023/3/17 9:49:00

最近,德国马克思普朗克医学研究所的Stefan W. Hell课题组取得了新的突破。他们利用MINFLUX技术剖析了kinesin-1的无障碍行走。相关成果已于2023年3月10日在国际权威学术期刊《科学》上发表。

该课题组引入了一种干涉式MINFLUX显微镜,可以以每毫秒1.7纳米的时空精度记录蛋白质的运动。相比之前需要在蛋白质上附着不成比例的大磁珠,MINFLUX仅需要检测约20个大小约为1纳米的荧光团的光子。因此,他们能够研究在生理腺苷-5'-三磷酸(ATP)浓度下,马达蛋白kinesin-1在微管上的步进。

研究人员发现在步进过程中无负载马达蛋白的茎部和头部会发生旋转,并表明ATP是由与微管结合的单个头部吸收的,当两个头部结合时发生ATP水解。他们的结果表明,MINFLUX以最小的干扰量化蛋白质的(亚)毫秒构象变化。

附:英文原文

Title: MINFLUX dissects the unimpeded walking of kinesin-1

Author: Jan O. Wolff, Lukas Scheiderer, Tobias Engelhardt, Johann Engelhardt, Jessica Matthias, Stefan W. Hell

Issue&Volume: 2023-03-10

Abstract: We introduce an interferometric MINFLUX microscope that records protein movements with up to 1.7 nanometer per millisecond spatiotemporal precision. Such precision has previously required attaching disproportionately large beads to the protein, but MINFLUX requires the detection of only about 20 photons from an approximately 1-nanometer-sized fluorophore. Therefore, we were able to study the stepping of the motor protein kinesin-1 on microtubules at up to physiological adenosine-5′-triphosphate (ATP) concentrations. We uncovered rotations of the stalk and the heads of load-free kinesin during stepping and showed that ATP is taken up with a single head bound to the microtubule and that ATP hydrolysis occurs when both heads are bound. Our results show that MINFLUX quantifies (sub)millisecond conformational changes of proteins with minimal disturbance.

DOI: ade2650

Source: https://www.science.org/doi/10.1126/science.ade2650

期刊信息
Science:《科学》,创刊于1880年。隶属于美国科学促进会,最新IF:63.714