Abstract
This work provides the first characteristics of the rhodopsin SpaR from Sphingomonas paucimobilis, aerobic bacteria associated with opportunistic infections. The sequence analysis of SpaR has shown that this protein has unusual DTS motif which has never reported in rhodopsins from Proteobacteria. We report that SpaR operates as an outward proton pump at low pH; however, proton pumping is almost absent at neutral and alkaline pH. The photocycle of this rhodopsin in detergent micelles slows down with an increase in pH because of longer Schiff base reprotonation. Our results show that the novel microbial ion transporter SpaR of interest both as an object for basic research of membrane proteins and as a promising optogenetic tool.
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24 April 2021
An Erratum to this paper has been published: https://doi.org/10.1134/S1607672921020198
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Funding
This work was partially supported by the Russian Foundation for Basic Research, project no. 17-00-00167K (KOMFI 17-00-00164, 17-00-00165, 17-00-00166).
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The authors declare that they have no conflict of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.
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N. Maliar, I.S. Okhrimenko, and L.E. Petrovskaya contributed equally to the work.
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Translated by M. Batrukova
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Maliar, N., Okhrimenko, I.S., Petrovskaya, L.E. et al. Novel pH-Sensitive Microbial Rhodopsin from Sphingomonas paucimobilis . Dokl Biochem Biophys 495, 342–346 (2020). https://doi.org/10.1134/S1607672920060162
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DOI: https://doi.org/10.1134/S1607672920060162