The temperature dependence of kinesin motor-protein mechanochemistry

Vandana S. Kushwaha; Erwin J.G. Peterman

doi:10.1016/j.bbrc.2020.06.004

The temperature dependence of kinesin motor-protein mechanochemistry

Vandana S. Kushwaha
, Erwin J.G. Peterman^*

^*Corresponding author for this work

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Biophysical studies of the mechanochemical cycle of kinesin motors are essential for understanding the mechanism of energy conversion. Here, we report a systematic study of the impact of temperature on velocity and run length of homodimeric Drosophila kinesin-1, homodimeric C. elegans OSM-3 and heterodimeric C. elegans kinesin-II motor proteins using in vitro single-molecule motility assays. Under saturated ATP conditions, kinesin-1 and OSM-3 are fast and processive motors compared to kinesin-II. From in vitro motility assays employing single-molecule fluorescence microscopy, we extracted single-motor velocities and run lengths in a temperature range from 15 °C to 35 °C. Both parameters showed a non-Arrhenius temperature dependence for all three motors, which could be quantitatively modeled using a simplified, two-state kinetic model of the mechanochemistry of the three motors, providing new insights in the temperature dependence of their mechanochemistry.

Original language	English
Pages (from-to)	812-818
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	529
Issue number	3
Early online date	30 Jun 2020
DOIs	https://doi.org/10.1016/j.bbrc.2020.06.004
Publication status	Published - 27 Aug 2020

Funding

This work was financially supported by the Netherlands Foundation for Scientific Research (NWO) via the grant “Barriers in the Brain” ( BIB, FOM-137 ) from the Foundation for Fundamental Research on Matter ( FOM ). This work was financially supported by the Netherlands Foundation for Scientific Research (NWO) via the grant ?Barriers in the Brain? (BIB, FOM-137) from the Foundation for Fundamental Research on Matter (FOM).

Funders	Funder number
Netherlands Foundation for Scientific Research
Stichting voor Fundamenteel Onderzoek der Materie
Nederlandse Organisatie voor Wetenschappelijk Onderzoek	FOM-137
Foundation for Fundamental Research on Matter

Keywords

ATP hydrolysis cycle
Caenorhabditis elegans
Kinesins
Microtubules
Motor proteins
Single molecule analysis
Single-molecule fluorescence microscopy
Temperature
TIRF microscopy

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title = "The temperature dependence of kinesin motor-protein mechanochemistry",

abstract = "Biophysical studies of the mechanochemical cycle of kinesin motors are essential for understanding the mechanism of energy conversion. Here, we report a systematic study of the impact of temperature on velocity and run length of homodimeric Drosophila kinesin-1, homodimeric C. elegans OSM-3 and heterodimeric C. elegans kinesin-II motor proteins using in vitro single-molecule motility assays. Under saturated ATP conditions, kinesin-1 and OSM-3 are fast and processive motors compared to kinesin-II. From in vitro motility assays employing single-molecule fluorescence microscopy, we extracted single-motor velocities and run lengths in a temperature range from 15 °C to 35 °C. Both parameters showed a non-Arrhenius temperature dependence for all three motors, which could be quantitatively modeled using a simplified, two-state kinetic model of the mechanochemistry of the three motors, providing new insights in the temperature dependence of their mechanochemistry.",

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N2 - Biophysical studies of the mechanochemical cycle of kinesin motors are essential for understanding the mechanism of energy conversion. Here, we report a systematic study of the impact of temperature on velocity and run length of homodimeric Drosophila kinesin-1, homodimeric C. elegans OSM-3 and heterodimeric C. elegans kinesin-II motor proteins using in vitro single-molecule motility assays. Under saturated ATP conditions, kinesin-1 and OSM-3 are fast and processive motors compared to kinesin-II. From in vitro motility assays employing single-molecule fluorescence microscopy, we extracted single-motor velocities and run lengths in a temperature range from 15 °C to 35 °C. Both parameters showed a non-Arrhenius temperature dependence for all three motors, which could be quantitatively modeled using a simplified, two-state kinetic model of the mechanochemistry of the three motors, providing new insights in the temperature dependence of their mechanochemistry.

AB - Biophysical studies of the mechanochemical cycle of kinesin motors are essential for understanding the mechanism of energy conversion. Here, we report a systematic study of the impact of temperature on velocity and run length of homodimeric Drosophila kinesin-1, homodimeric C. elegans OSM-3 and heterodimeric C. elegans kinesin-II motor proteins using in vitro single-molecule motility assays. Under saturated ATP conditions, kinesin-1 and OSM-3 are fast and processive motors compared to kinesin-II. From in vitro motility assays employing single-molecule fluorescence microscopy, we extracted single-motor velocities and run lengths in a temperature range from 15 °C to 35 °C. Both parameters showed a non-Arrhenius temperature dependence for all three motors, which could be quantitatively modeled using a simplified, two-state kinetic model of the mechanochemistry of the three motors, providing new insights in the temperature dependence of their mechanochemistry.

KW - ATP hydrolysis cycle

KW - Caenorhabditis elegans

KW - Kinesins

KW - Microtubules

KW - Motor proteins

KW - Single molecule analysis

KW - Single-molecule fluorescence microscopy

KW - Temperature

KW - TIRF microscopy

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The temperature dependence of kinesin motor-protein mechanochemistry

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