The temperature dependence of kinesin motor-protein mechanochemistry

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

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review


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 languageEnglish
Pages (from-to)812-818
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Early online date30 Jun 2020
Publication statusPublished - 27 Aug 2020


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 ).

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


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


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