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Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes
BACKGROUND: Green fluorescent protein (GFP) has been found in a wide range of Cnidaria, a basal group of metazoans in which it is associated with pigmentation, fluorescence, and light absorbance. A GFP has been recently discovered in the pigmentless chordate Branchiostoma floridae (amphioxus) that s...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2679011/ https://www.ncbi.nlm.nih.gov/pubmed/19379521 http://dx.doi.org/10.1186/1471-2148-9-77 |
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author | Bomati, Erin K Manning, Gerard Deheyn, Dimitri D |
author_facet | Bomati, Erin K Manning, Gerard Deheyn, Dimitri D |
author_sort | Bomati, Erin K |
collection | PubMed |
description | BACKGROUND: Green fluorescent protein (GFP) has been found in a wide range of Cnidaria, a basal group of metazoans in which it is associated with pigmentation, fluorescence, and light absorbance. A GFP has been recently discovered in the pigmentless chordate Branchiostoma floridae (amphioxus) that shows intense fluorescence mainly in the head region. RESULTS: The amphioxus genome encodes 16 closely-related GFP-like proteins, all of which appear to be under purifying selection. We divide them into 6 clades based on protein sequence identity and show that representatives of each clade have significant differences in fluorescence intensity, extinction coefficients, and absorption profiles. Furthermore, GFPs from two clades exhibit antioxidant capacity. We therefore propose that amphioxus GFPs have diversified their functions into fluorescence, redox, and perhaps just light absorption in relation to pigmentation and/or photoprotection. CONCLUSION: The rapid radiation of amphioxus GFP into clades with distinct functions and spectral properties reveals functional plasticity of the GFP core. The high sequence similarities between different clades provide a model system to map sequence variation to functional changes, to better understand and engineer GFP. |
format | Text |
id | pubmed-2679011 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-26790112009-05-08 Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes Bomati, Erin K Manning, Gerard Deheyn, Dimitri D BMC Evol Biol Research Article BACKGROUND: Green fluorescent protein (GFP) has been found in a wide range of Cnidaria, a basal group of metazoans in which it is associated with pigmentation, fluorescence, and light absorbance. A GFP has been recently discovered in the pigmentless chordate Branchiostoma floridae (amphioxus) that shows intense fluorescence mainly in the head region. RESULTS: The amphioxus genome encodes 16 closely-related GFP-like proteins, all of which appear to be under purifying selection. We divide them into 6 clades based on protein sequence identity and show that representatives of each clade have significant differences in fluorescence intensity, extinction coefficients, and absorption profiles. Furthermore, GFPs from two clades exhibit antioxidant capacity. We therefore propose that amphioxus GFPs have diversified their functions into fluorescence, redox, and perhaps just light absorption in relation to pigmentation and/or photoprotection. CONCLUSION: The rapid radiation of amphioxus GFP into clades with distinct functions and spectral properties reveals functional plasticity of the GFP core. The high sequence similarities between different clades provide a model system to map sequence variation to functional changes, to better understand and engineer GFP. BioMed Central 2009-04-21 /pmc/articles/PMC2679011/ /pubmed/19379521 http://dx.doi.org/10.1186/1471-2148-9-77 Text en Copyright © 2009 Bomati et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Bomati, Erin K Manning, Gerard Deheyn, Dimitri D Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes |
title | Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes |
title_full | Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes |
title_fullStr | Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes |
title_full_unstemmed | Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes |
title_short | Amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes |
title_sort | amphioxus encodes the largest known family of green fluorescent proteins, which have diversified into distinct functional classes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2679011/ https://www.ncbi.nlm.nih.gov/pubmed/19379521 http://dx.doi.org/10.1186/1471-2148-9-77 |
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