The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes

Abstract Background The process of photoreception in most animals depends on the light induced isomerization of the chromophore retinal, bound to rhodopsin. To re-use retinal, the all-trans-retinal form needs to be re-isomerized to 11-cis-retinal, which can be achieved in different ways. In vertebra...

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Autores principales:	Oliver Vöcking, Lucas Leclère, Harald Hausen
Formato:	article
Lenguaje:	EN
Publicado:	BMC 2021
Materias:	Opsin Retinochrome RALBP RLBP1 Visual cycle Mollusk Ecology QH540-549.5 Evolution QH359-425
Acceso en línea:	https://doaj.org/article/18e38965eb4c45edb812396d5b9e342c
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spelling	oai:doaj.org-article:18e38965eb4c45edb812396d5b9e342c2021-12-05T12:04:14ZThe rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes10.1186/s12862-021-01939-x2730-7182https://doaj.org/article/18e38965eb4c45edb812396d5b9e342c2021-11-01T00:00:00Zhttps://doi.org/10.1186/s12862-021-01939-xhttps://doaj.org/toc/2730-7182Abstract Background The process of photoreception in most animals depends on the light induced isomerization of the chromophore retinal, bound to rhodopsin. To re-use retinal, the all-trans-retinal form needs to be re-isomerized to 11-cis-retinal, which can be achieved in different ways. In vertebrates, this mostly includes a stepwise enzymatic process called the visual cycle. The best studied re-isomerization system in protostomes is the rhodopsin-retinochrome system of cephalopods, which consists of rhodopsin, the photoisomerase retinochrome and the protein RALBP functioning as shuttle for retinal. In this study we investigate the expression of the rhodopsin-retinochrome system and functional components of the vertebrate visual cycle in a polyplacophoran mollusk, Leptochiton asellus, and examine the phylogenetic distribution of the individual components in other protostome animals. Results Tree-based orthology assignments revealed that orthologs of the cephalopod retinochrome and RALBP are present in mollusks outside of cephalopods. By mining our dataset for vertebrate visual cycle components, we also found orthologs of the retinoid binding protein RLBP1, in polyplacophoran mollusks, cephalopods and a phoronid. In situ hybridization and antibody staining revealed that L. asellus retinochrome is co-expressed in the larval chiton photoreceptor cells (PRCs) with the visual rhodopsin, RALBP and RLBP1. In addition, multiple retinal dehydrogenases are expressed in the PRCs, which might also contribute to the rhodopsin-retinochrome system. Conclusions We conclude that the rhodopsin-retinochrome system is a common feature of mollusk PRCs and predates the origin of cephalopod eyes. Our results show that this system has to be extended by adding further components, which surprisingly, are shared with vertebrates.Oliver VöckingLucas LeclèreHarald HausenBMCarticleOpsinRetinochromeRALBPRLBP1Visual cycleMolluskEcologyQH540-549.5EvolutionQH359-425ENBMC Ecology and Evolution, Vol 21, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Opsin Retinochrome RALBP RLBP1 Visual cycle Mollusk Ecology QH540-549.5 Evolution QH359-425
spellingShingle	Opsin Retinochrome RALBP RLBP1 Visual cycle Mollusk Ecology QH540-549.5 Evolution QH359-425 Oliver Vöcking Lucas Leclère Harald Hausen The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes
description	Abstract Background The process of photoreception in most animals depends on the light induced isomerization of the chromophore retinal, bound to rhodopsin. To re-use retinal, the all-trans-retinal form needs to be re-isomerized to 11-cis-retinal, which can be achieved in different ways. In vertebrates, this mostly includes a stepwise enzymatic process called the visual cycle. The best studied re-isomerization system in protostomes is the rhodopsin-retinochrome system of cephalopods, which consists of rhodopsin, the photoisomerase retinochrome and the protein RALBP functioning as shuttle for retinal. In this study we investigate the expression of the rhodopsin-retinochrome system and functional components of the vertebrate visual cycle in a polyplacophoran mollusk, Leptochiton asellus, and examine the phylogenetic distribution of the individual components in other protostome animals. Results Tree-based orthology assignments revealed that orthologs of the cephalopod retinochrome and RALBP are present in mollusks outside of cephalopods. By mining our dataset for vertebrate visual cycle components, we also found orthologs of the retinoid binding protein RLBP1, in polyplacophoran mollusks, cephalopods and a phoronid. In situ hybridization and antibody staining revealed that L. asellus retinochrome is co-expressed in the larval chiton photoreceptor cells (PRCs) with the visual rhodopsin, RALBP and RLBP1. In addition, multiple retinal dehydrogenases are expressed in the PRCs, which might also contribute to the rhodopsin-retinochrome system. Conclusions We conclude that the rhodopsin-retinochrome system is a common feature of mollusk PRCs and predates the origin of cephalopod eyes. Our results show that this system has to be extended by adding further components, which surprisingly, are shared with vertebrates.
format	article
author	Oliver Vöcking Lucas Leclère Harald Hausen
author_facet	Oliver Vöcking Lucas Leclère Harald Hausen
author_sort	Oliver Vöcking
title	The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes
title_short	The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes
title_full	The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes
title_fullStr	The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes
title_full_unstemmed	The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes
title_sort	rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes
publisher	BMC
publishDate	2021
url	https://doaj.org/article/18e38965eb4c45edb812396d5b9e342c
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The rhodopsin-retinochrome system for retinal re-isomerization predates the origin of cephalopod eyes

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