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Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types

The position of carotenoid in xanthorhodopsin has been elucidated. However, a challenging expression of this opsin and a complex biosynthesis carotenoid in the laboratory hold back the insightful study of this rhodopsin. Here, we demonstrated co-expression of the xanthorhodopsin type isolated from G...

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Autores principales: Chuon, Kimleng, Shim, Jin-gon, Kang, Kun-Wook, Cho, Shin-Gyu, Hour, Chenda, Meas, Seanghun, Kim, Ji-Hyun, Choi, Ahreum, Jung, Kwang-Hwan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9151804/
https://www.ncbi.nlm.nih.gov/pubmed/35637261
http://dx.doi.org/10.1038/s42003-022-03429-2
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author Chuon, Kimleng
Shim, Jin-gon
Kang, Kun-Wook
Cho, Shin-Gyu
Hour, Chenda
Meas, Seanghun
Kim, Ji-Hyun
Choi, Ahreum
Jung, Kwang-Hwan
author_facet Chuon, Kimleng
Shim, Jin-gon
Kang, Kun-Wook
Cho, Shin-Gyu
Hour, Chenda
Meas, Seanghun
Kim, Ji-Hyun
Choi, Ahreum
Jung, Kwang-Hwan
author_sort Chuon, Kimleng
collection PubMed
description The position of carotenoid in xanthorhodopsin has been elucidated. However, a challenging expression of this opsin and a complex biosynthesis carotenoid in the laboratory hold back the insightful study of this rhodopsin. Here, we demonstrated co-expression of the xanthorhodopsin type isolated from Gloeobacter violaceus PCC 7421-Gloeobacter rhodopsin (GR) with a biosynthesized keto-carotenoid (canthaxanthin) targeting the carotenoid binding site. Direct mutation-induced changes in carotenoid-rhodopsin interaction revealed three crucial features: (1) carotenoid locked motif (CLM), (2) carotenoid aligned motif (CAM), and color tuning serines (CTS). Our single mutation results at 178 position (G178W) confirmed inhibition of carotenoid binding; however, the mutants showed better stability and proton pumping, which was also observed in the case of carotenoid binding characteristics. These effects demonstrated an adaptation of microbial rhodopsin that diverges from carotenoid harboring, along with expression in the dinoflagellate Pyrocystis lunula rhodopsin and the evolutionary substitution model. The study highlights a critical position of the carotenoid binding site, which significantly allows another protein engineering approach in the microbial rhodopsin family.
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spelling pubmed-91518042022-06-01 Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types Chuon, Kimleng Shim, Jin-gon Kang, Kun-Wook Cho, Shin-Gyu Hour, Chenda Meas, Seanghun Kim, Ji-Hyun Choi, Ahreum Jung, Kwang-Hwan Commun Biol Article The position of carotenoid in xanthorhodopsin has been elucidated. However, a challenging expression of this opsin and a complex biosynthesis carotenoid in the laboratory hold back the insightful study of this rhodopsin. Here, we demonstrated co-expression of the xanthorhodopsin type isolated from Gloeobacter violaceus PCC 7421-Gloeobacter rhodopsin (GR) with a biosynthesized keto-carotenoid (canthaxanthin) targeting the carotenoid binding site. Direct mutation-induced changes in carotenoid-rhodopsin interaction revealed three crucial features: (1) carotenoid locked motif (CLM), (2) carotenoid aligned motif (CAM), and color tuning serines (CTS). Our single mutation results at 178 position (G178W) confirmed inhibition of carotenoid binding; however, the mutants showed better stability and proton pumping, which was also observed in the case of carotenoid binding characteristics. These effects demonstrated an adaptation of microbial rhodopsin that diverges from carotenoid harboring, along with expression in the dinoflagellate Pyrocystis lunula rhodopsin and the evolutionary substitution model. The study highlights a critical position of the carotenoid binding site, which significantly allows another protein engineering approach in the microbial rhodopsin family. Nature Publishing Group UK 2022-05-30 /pmc/articles/PMC9151804/ /pubmed/35637261 http://dx.doi.org/10.1038/s42003-022-03429-2 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Chuon, Kimleng
Shim, Jin-gon
Kang, Kun-Wook
Cho, Shin-Gyu
Hour, Chenda
Meas, Seanghun
Kim, Ji-Hyun
Choi, Ahreum
Jung, Kwang-Hwan
Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types
title Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types
title_full Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types
title_fullStr Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types
title_full_unstemmed Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types
title_short Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types
title_sort carotenoid binding in gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9151804/
https://www.ncbi.nlm.nih.gov/pubmed/35637261
http://dx.doi.org/10.1038/s42003-022-03429-2
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