Adaptation of Antarctic Icefish Vision to Extreme Environments

Abstract 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 o...

Full description

Bibliographic Details
Published in:Molecular Biology and Evolution
Main Authors: Castiglione, Gianni M, Hauser, Frances E, Van Nynatten, Alexander, Chang, Belinda S W
Other Authors: Yang, Guang
Format: Article in Journal/Newspaper
Language:English
Published: Oxford University Press (OUP) 2023
Subjects:
Online Access:http://dx.doi.org/10.1093/molbev/msad030
https://academic.oup.com/mbe/advance-article-pdf/doi/10.1093/molbev/msad030/49157101/msad030.pdf
https://academic.oup.com/mbe/article-pdf/40/4/msad030/50388900/msad030.pdf
id croxfordunivpr:10.1093/molbev/msad030
record_format openpolar
spelling croxfordunivpr:10.1093/molbev/msad030 2024-05-19T07:31:49+00:00 Adaptation of Antarctic Icefish Vision to Extreme Environments Castiglione, Gianni M Hauser, Frances E Van Nynatten, Alexander Chang, Belinda S W Yang, Guang 2023 http://dx.doi.org/10.1093/molbev/msad030 https://academic.oup.com/mbe/advance-article-pdf/doi/10.1093/molbev/msad030/49157101/msad030.pdf https://academic.oup.com/mbe/article-pdf/40/4/msad030/50388900/msad030.pdf en eng Oxford University Press (OUP) https://creativecommons.org/licenses/by-nc/4.0/ Molecular Biology and Evolution volume 40, issue 4 ISSN 0737-4038 1537-1719 journal-article 2023 croxfordunivpr https://doi.org/10.1093/molbev/msad030 2024-05-02T09:30:09Z Abstract 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. Article in Journal/Newspaper Antarc* Antarctic Icefish Sea ice Oxford University Press Molecular Biology and Evolution
institution Open Polar
collection Oxford University Press
op_collection_id croxfordunivpr
language English
description Abstract 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.
author2 Yang, Guang
format Article in Journal/Newspaper
author Castiglione, Gianni M
Hauser, Frances E
Van Nynatten, Alexander
Chang, Belinda S W
spellingShingle Castiglione, Gianni M
Hauser, Frances E
Van Nynatten, Alexander
Chang, Belinda S W
Adaptation of Antarctic Icefish Vision to Extreme Environments
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 (OUP)
publishDate 2023
url http://dx.doi.org/10.1093/molbev/msad030
https://academic.oup.com/mbe/advance-article-pdf/doi/10.1093/molbev/msad030/49157101/msad030.pdf
https://academic.oup.com/mbe/article-pdf/40/4/msad030/50388900/msad030.pdf
genre Antarc*
Antarctic
Icefish
Sea ice
genre_facet Antarc*
Antarctic
Icefish
Sea ice
op_source Molecular Biology and Evolution
volume 40, issue 4
ISSN 0737-4038 1537-1719
op_rights https://creativecommons.org/licenses/by-nc/4.0/
op_doi https://doi.org/10.1093/molbev/msad030
container_title Molecular Biology and Evolution
_version_ 1799469708360024064