Adaptation of Antarctic Icefish Vision to Extreme Environments
Extreme environments, such as Antarctic habitats, present major challenges for many biological processes. Antarctic icefishes (Crynotothenioidea) represent a compelling system to investigate the molecular basis of adaptation to cold temperatures. Here, we explore how the sub-zero habitats of Antarct...
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2023
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Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10097508/ http://www.ncbi.nlm.nih.gov/pubmed/36763103 https://doi.org/10.1093/molbev/msad030 |
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ftpubmed:oai:pubmedcentral.nih.gov:10097508 2023-06-06T11:47:30+02:00 Adaptation of Antarctic Icefish Vision to Extreme Environments Castiglione, Gianni M Hauser, Frances E Van Nynatten, Alexander Chang, Belinda S W 2023-02-10 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10097508/ http://www.ncbi.nlm.nih.gov/pubmed/36763103 https://doi.org/10.1093/molbev/msad030 en eng Oxford University Press http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10097508/ http://www.ncbi.nlm.nih.gov/pubmed/36763103 http://dx.doi.org/10.1093/molbev/msad030 © The Author(s) 2023. Published by Oxford University Press on behalf of Society for Molecular Biology and Evolution. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com Mol Biol Evol Discoveries Text 2023 ftpubmed https://doi.org/10.1093/molbev/msad030 2023-04-16T01:25:46Z Extreme environments, such as Antarctic habitats, present major challenges for many biological processes. Antarctic icefishes (Crynotothenioidea) represent a compelling system to investigate the molecular basis of adaptation to cold temperatures. Here, we explore how the sub-zero habitats of Antarctic icefishes have impacted rhodopsin (RH1) function, the temperature-sensitive dim-light visual pigment found in rod photoreceptors. Using likelihood models and ancestral reconstruction, we find that accelerated evolutionary rates in icefish RH1 underlie unique amino acid mutations absent from other deep-dwelling fishes, introduced before (S160A) and during (V259M) the onset of modern polar conditions. Functional assays reveal that these mutations red-shift rhodopsin spectral absorbance, consistent with spectral irradiance under sea ice. These mutations also lower the activation energy associated with retinal release of the light-activated RH1, and accelerate its return to the dark state, likely compensating for a cold-induced decrease in kinetic rates. These are adaptations in key properties of rhodopsin that mediate rod sensitivity and visual performance in the cold dark seas of the Antarctic. Text Antarc* Antarctic Icefish Sea ice PubMed Central (PMC) Antarctic The Antarctic Molecular Biology and Evolution 40 4 |
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Discoveries Castiglione, Gianni M Hauser, Frances E Van Nynatten, Alexander Chang, Belinda S W Adaptation of Antarctic Icefish Vision to Extreme Environments |
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Discoveries |
description |
Extreme environments, such as Antarctic habitats, present major challenges for many biological processes. Antarctic icefishes (Crynotothenioidea) represent a compelling system to investigate the molecular basis of adaptation to cold temperatures. Here, we explore how the sub-zero habitats of Antarctic icefishes have impacted rhodopsin (RH1) function, the temperature-sensitive dim-light visual pigment found in rod photoreceptors. Using likelihood models and ancestral reconstruction, we find that accelerated evolutionary rates in icefish RH1 underlie unique amino acid mutations absent from other deep-dwelling fishes, introduced before (S160A) and during (V259M) the onset of modern polar conditions. Functional assays reveal that these mutations red-shift rhodopsin spectral absorbance, consistent with spectral irradiance under sea ice. These mutations also lower the activation energy associated with retinal release of the light-activated RH1, and accelerate its return to the dark state, likely compensating for a cold-induced decrease in kinetic rates. These are adaptations in key properties of rhodopsin that mediate rod sensitivity and visual performance in the cold dark seas of the Antarctic. |
format |
Text |
author |
Castiglione, Gianni M Hauser, Frances E Van Nynatten, Alexander Chang, Belinda S W |
author_facet |
Castiglione, Gianni M Hauser, Frances E Van Nynatten, Alexander Chang, Belinda S W |
author_sort |
Castiglione, Gianni M |
title |
Adaptation of Antarctic Icefish Vision to Extreme Environments |
title_short |
Adaptation of Antarctic Icefish Vision to Extreme Environments |
title_full |
Adaptation of Antarctic Icefish Vision to Extreme Environments |
title_fullStr |
Adaptation of Antarctic Icefish Vision to Extreme Environments |
title_full_unstemmed |
Adaptation of Antarctic Icefish Vision to Extreme Environments |
title_sort |
adaptation of antarctic icefish vision to extreme environments |
publisher |
Oxford University Press |
publishDate |
2023 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10097508/ http://www.ncbi.nlm.nih.gov/pubmed/36763103 https://doi.org/10.1093/molbev/msad030 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Icefish Sea ice |
genre_facet |
Antarc* Antarctic Icefish Sea ice |
op_source |
Mol Biol Evol |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10097508/ http://www.ncbi.nlm.nih.gov/pubmed/36763103 http://dx.doi.org/10.1093/molbev/msad030 |
op_rights |
© The Author(s) 2023. Published by Oxford University Press on behalf of Society for Molecular Biology and Evolution. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
op_doi |
https://doi.org/10.1093/molbev/msad030 |
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Molecular Biology and Evolution |
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40 |
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4 |
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1767952940518080512 |