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      Non-excitable fluorescent protein orthologs found in ctenophores

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          Abstract

          Background

          Fluorescent proteins are optically active proteins found across many clades in metazoans. A fluorescent protein was recently identified in a ctenophore, but this has been suggested to derive from a cnidarian, raising again the question of origins of this group of proteins.

          Results

          Through analysis of transcriptome data from 30 ctenophores, we identified a member of an orthologous group of proteins similar to fluorescent proteins in each of them, as well as in the genome of Mnemiopsis leidyi. These orthologs lack canonical residues involved in chromophore formation, suggesting another function.

          Conclusions

          The phylogenetic position of the ctenophore protein family among fluorescent proteins suggests that this gene was present in the common ancestor of all ctenophores and that the fluorescent protein previously found in a ctenophore actually derives from a siphonophore.

          Electronic supplementary material

          The online version of this article (doi:10.1186/s12862-016-0738-5) contains supplementary material, which is available to authorized users.

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          Most cited references6

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          Advances in fluorescent protein technology.

          Current fluorescent protein (FP) development strategies are focused on fine-tuning the photophysical properties of blue to yellow variants derived from the Aequorea victoria jellyfish green fluorescent protein (GFP) and on the development of monomeric FPs from other organisms that emit in the yellow-orange to far-red regions of the visible light spectrum. Progress toward these goals has been substantial, and near-infrared emitting FPs may loom over the horizon. The latest efforts in jellyfish variants have resulted in new and improved monomeric BFP, CFP, GFP and YFP variants, and the relentless search for a bright, monomeric and fast-maturing red FP has yielded a host of excellent candidates, although none is yet optimal for all applications. Meanwhile, photoactivatable FPs are emerging as a powerful class of probes for intracellular dynamics and, unexpectedly, as useful tools for the development of superresolution microscopy applications.
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            Evolution of coral pigments recreated.

            In proteins homologous to the green fluorescent protein (GFP), formation of red fluorescence requires three autocatalytic steps, whereas only two are needed for green fluorescence. Multiple red/green color diversification events in the GFP superfamily may reflect convergent evolution of the more complex three-step pathway. In the great star coral Montastraea cavernosa, a recreated common ancestor of green and red proteins turned out to be green, indicating that in this case red proteins evolved their color independently from most other homologous red proteins. Furthermore, red color appears to have evolved gradually by small incremental transitions.
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              • Article: not found

              Endogenous green fluorescent protein (GFP) in amphioxus.

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                Author and article information

                Contributors
                wrf@lrz.uni-muenchen.de
                lynne@mbari.org
                Meghan.Powers@waterboards.ca.gov
                christine.schnitzler@nih.gov
                haddock@mbari.org
                Journal
                BMC Evol Biol
                BMC Evol. Biol
                BMC Evolutionary Biology
                BioMed Central (London )
                1471-2148
                24 August 2016
                24 August 2016
                2016
                : 16
                : 1
                : 167
                Affiliations
                [1 ]Monterey Bay Aquarium Research Institute, 7700 Sandholdt Rd., 95039 Moss Landing, USA
                [2 ]National Human Genome Research Institute, National Institutes of Health, 50 South Drive, Bethesda, 20892 USA
                [3 ]Present address: Ludwig-Maximilians-Universität München, Munich, Germany
                [4 ]Present address: Whitney Laboratory for Marine Bioscience, University of Florida, St. Augustine, Florida, 32080 USA
                Article
                738
                10.1186/s12862-016-0738-5
                4997694
                27557948
                ffcdaa68-7643-4629-b743-00d249a14c67
                © The Author(s) 2016

                Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                : 25 January 2016
                : 9 August 2016
                Funding
                Funded by: National Institute of General Medical Sciences
                Award ID: 5-R01-GM087198
                Categories
                Research Article
                Custom metadata
                © The Author(s) 2016

                Evolutionary Biology
                fluorescent protein,ctenophore,siphonophore,transcriptome,fluorescence,haeckelia
                Evolutionary Biology
                fluorescent protein, ctenophore, siphonophore, transcriptome, fluorescence, haeckelia

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