Electrophoretic Deformation of Individual Transfer RNA Molecules Reveals Their Identity

Robert Y. Henley; Brian Alan Ashcroft; Ian Farrell; Barry S. Cooperman; Stuart Lindsay; Meni Wanunu

doi:10.1021/acs.nanolett.5b03331

Electrophoretic Deformation of Individual Transfer RNA Molecules Reveals Their Identity

Robert Y. Henley, Brian Alan Ashcroft, Ian Farrell, Barry S. Cooperman, Stuart Lindsay, Meni Wanunu

Research output: Contribution to journal › Article › peer-review

36 Scopus citations

Abstract

It has been hypothesized that the ribosome gains additional fidelity during protein translation by probing structural differences in tRNA species. We measure the translocation kinetics of different tRNA species through ∼3 nm diameter synthetic nanopores. Each tRNA species varies in the time scale with which it is deformed from equilibrium, as in the translocation step of protein translation. Using machine-learning algorithms, we can differentiate among five tRNA species, analyze the ratios of tRNA binary mixtures, and distinguish tRNA isoacceptors. (Figure Presented).

Original language	English (US)
Pages (from-to)	138-144
Number of pages	7
Journal	Nano Letters
Volume	16
Issue number	1
DOIs	https://doi.org/10.1021/acs.nanolett.5b03331
State	Published - Jan 13 2016

Keywords

RNA
SVM
nanopores
single molecule
tRNA

ASJC Scopus subject areas

Bioengineering
Chemistry(all)
Materials Science(all)
Condensed Matter Physics
Mechanical Engineering

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10.1021/acs.nanolett.5b03331

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abstract = "It has been hypothesized that the ribosome gains additional fidelity during protein translation by probing structural differences in tRNA species. We measure the translocation kinetics of different tRNA species through ∼3 nm diameter synthetic nanopores. Each tRNA species varies in the time scale with which it is deformed from equilibrium, as in the translocation step of protein translation. Using machine-learning algorithms, we can differentiate among five tRNA species, analyze the ratios of tRNA binary mixtures, and distinguish tRNA isoacceptors. (Figure Presented).",

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AU - Henley, Robert Y.

AU - Ashcroft, Brian Alan

AU - Farrell, Ian

AU - Cooperman, Barry S.

AU - Lindsay, Stuart

AU - Wanunu, Meni

N1 - Funding Information: We acknowledge support from the National Institutes of Health for this work (HG006873, MW; HG 006323, SML; GM080376, BSC). Publisher Copyright: © 2015 American Chemical Society.

PY - 2016/1/13

Y1 - 2016/1/13

N2 - It has been hypothesized that the ribosome gains additional fidelity during protein translation by probing structural differences in tRNA species. We measure the translocation kinetics of different tRNA species through ∼3 nm diameter synthetic nanopores. Each tRNA species varies in the time scale with which it is deformed from equilibrium, as in the translocation step of protein translation. Using machine-learning algorithms, we can differentiate among five tRNA species, analyze the ratios of tRNA binary mixtures, and distinguish tRNA isoacceptors. (Figure Presented).

AB - It has been hypothesized that the ribosome gains additional fidelity during protein translation by probing structural differences in tRNA species. We measure the translocation kinetics of different tRNA species through ∼3 nm diameter synthetic nanopores. Each tRNA species varies in the time scale with which it is deformed from equilibrium, as in the translocation step of protein translation. Using machine-learning algorithms, we can differentiate among five tRNA species, analyze the ratios of tRNA binary mixtures, and distinguish tRNA isoacceptors. (Figure Presented).

KW - RNA

KW - SVM

KW - nanopores

KW - single molecule

KW - tRNA

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Electrophoretic Deformation of Individual Transfer RNA Molecules Reveals Their Identity

Abstract

Keywords

ASJC Scopus subject areas

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