Photocontrol of small GTPase Ras fused with a photoresponsive protein.
| Autor: | Nishibe N; Department of Biosciences, Graduate School of Science and Engineering Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, Japan., Maruta S; Department of Biosciences, Graduate School of Science and Engineering Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577, Japan. |
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| Jazyk: | angličtina |
| Zdroj: | Journal of biochemistry [J Biochem] 2024 Jul 01; Vol. 176 (1), pp. 11-21. |
| DOI: | 10.1093/jb/mvae017 |
| Abstrakt: | The small GTPase Ras plays an important role in intracellular signal transduction and functions as a molecular switch. In this study, we used a photoresponsive protein as the molecular regulatory device to photoregulate Ras GTPase activity. Photo zipper (PZ), a variant of the photoresponsive protein Aureochrome1 developed by Hisatomi et al. was incorporated into the C-terminus of Ras as a fusion protein. The three constructs of the Ras-PZ fusion protein had spacers of different lengths between Ras and PZ. They were designed using an Escherichia coli expression system. The Ras-PZ fusion proteins exhibited photoisomerization upon blue light irradiation and in the dark. Ras-PZ dimerized upon light irradiation. Moreover, Ras GTPase activity, which is accelerated by the Ras regulators guanine nucleotide exchange factors and GTPase-activating proteins, is controlled by photoisomerization. It has been suggested that light-responsive proteins are applicable to the photoswitching of the enzymatic activity of small GTPases as photoregulatory molecular devices. (© The Author(s) 2024. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.) |
| Databáze: | MEDLINE |
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