Abstract
Movement is a fundamental characteristic of all living things. This biogenic function is carried out by various nanometer-sized molecular machines. Molecular motor is a typical molecular machinery in which the characteristic features of proteins are integrated; these include enzymatic activity, energy conversion, molecular recognition and self-assembly. These biologically important reactions occur with the association of water molecules that surround the motors. Applied pressures can alter the intermolecular interactions between the motors and water. In this chapter we describe the development of a high-pressure microscope and a new motility assay that enables the visualization of the motility of molecular motors under conditions of high-pressure. Our results demonstrate that applied pressure dynamically changes the motility of molecular motors such as kinesin, F1-ATPase and bacterial flagellar motors.
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Acknowledgments
We would like to thank Tomoko Miyata for providing an Electron micrograph of E. coli (Fig. 27.5a), Akihiko Ishijima for illustrating a computer graphics of flagellar motor (Fig. 27.6). Yoshifumi Kimura for developing high-pressure chamber for microscopy, Daichi Okuno and Hiroyuki Noji for the measurement of F1-ATPase, Yoshiyuki Sowa for the measurement of flagellar motors, Michio Homma, Akihiko Ishijima, Masahide Terazima and Yoshie Harada for technical support and discussion. This work was supported by PRESTO from JST, Grants-in-Aid for Scientific Research from MEXT and Shimadzu Science Foundation.
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Nishiyama, M. (2015). High-Pressure Microscopy for Studying Molecular Motors. In: Akasaka, K., Matsuki, H. (eds) High Pressure Bioscience. Subcellular Biochemistry, vol 72. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9918-8_27
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