Rational engineering of DNA-nanoparticle motor with high speed and processivity comparable to motor proteins

DNA-nanoparticle motor is a burnt-bridge Brownian ratchet moving on RNA-modified surface driven by Ribonuclease H (RNase H), and one of the fastest nanoscale artificial motors. However, its speed is still much lower than those of motor proteins. Here we resolve elementary processes of motion and reveal long pauses caused by slow RNase H binding are the bottleneck. As RNase H concentration ([RNase H]) increases, pause lengths shorten from ~70 s to ~0.2 s, while step sizes (displacements between two consecutive pauses) are constant ( ~ 20 nm). At high [RNase H], speed reaches ~100 nm s<sup>-1</sup>, however, processivity (total number of steps before detachment), run-length, and unidirectionality largely decrease. A geometry-based kinetic simulation reveals switching of bottleneck from RNase H binding to DNA/RNA hybridization at high [RNase H], and trade-off mechanism between speed and other performances. An engineered motor with 3.8-times larger DNA/RNA hybridization rate simultaneously achieves 30 nm s<sup>-1</sup> speed, 200 processivity, and 3 μm run-length comparable to motor proteins.

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Publication Details

Journal
Nature Communications
Published
2025-01-16
DOI
https://doi.org/10.1038/s41467-025-56036-0
Citations
6
Primary Topic
Advanced biosensing and bioanalysis techniques
Type
article
Field-Weighted Citation Impact
4.84

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article

Rational engineering of DNA-nanoparticle motor with high speed and processivity comparable to motor proteins

A. Otomo, Ryota Iino, Takanori Harashima
6 citations
Nature Communications
Advanced biosensing and bioanalysis techniques
4.84
article

Rational engineering of DNA-nanoparticle motor with high speed and processivity comparable to motor proteins

A. Otomo, Ryota Iino, Takanori Harashima
article en
6 citations

Abstract

DNA-nanoparticle motor is a burnt-bridge Brownian ratchet moving on RNA-modified surface driven by Ribonuclease H (RNase H), and one of the fastest nanoscale artificial motors. However, its speed is still much lower than those of motor proteins. Here we resolve elementary processes of motion and reveal long pauses caused by slow RNase H binding are the bottleneck. As RNase H concentration ([RNase H]) increases, pause lengths shorten from ~70 s to ~0.2 s, while step sizes (displacements between two consecutive pauses) are constant ( ~ 20 nm). At high [RNase H], speed reaches ~100 nm s<sup>-1</sup>, however, processivity (total number of steps before detachment), run-length, and unidirectionality largely decrease. A geometry-based kinetic simulation reveals switching of bottleneck from RNase H binding to DNA/RNA hybridization at high [RNase H], and trade-off mechanism between speed and other performances. An engineered motor with 3.8-times larger DNA/RNA hybridization rate simultaneously achieves 30 nm s<sup>-1</sup> speed, 200 processivity, and 3 μm run-length comparable to motor proteins.

Nature CommunicationsVol. 16(1)
National Institutes of Natural Sciences (JP), The Graduate University for Advanced Studies, SOKENDAI (JP), Institute for Molecular Science (JP)
Tsugawa Motor Kenkyu Foundation, Japan Society for the Promotion of Science, Japan Science and Technology Agency, ACT-X
Openalex Percentile: Top 6%
Advanced biosensing and bioanalysis techniques
4.84
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Rational engineering of DNA-nanoparticle motor with high speed and processivity comparable to motor proteins — A. Otomo, Ryota Iino, et al. · Nature Communications (2025) | TGRS Research Map | TGRS