Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin
Like many aquatic vertebrates, whales have blue-shifting spectral tuning substitutions in the dim-light visual pigment, rhodopsin, that are thought to increase photosensitivity in underwater environments. We have discovered that known spectral tuning substitutions also have surprising epistatic effe...
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Online Access: | https://doi.org/10.5061/dryad.5k0s6 |
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fttriple:oai:gotriple.eu:50|dedup_wf_001::f93edf35c2a02f27ae95c7269ab233e4 2023-05-15T17:03:32+02:00 Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin Dungan, Sarah Z. Chang, Belinda S. W. 2017-01-01 https://doi.org/10.5061/dryad.5k0s6 undefined unknown Data Archiving and Networked Services (DANS) http://dx.doi.org/10.5061/dryad.5k0s6 https://dx.doi.org/10.5061/dryad.5k0s6 lic_creative-commons oai:easy.dans.knaw.nl:easy-dataset:101014 10.5061/dryad.5k0s6 oai:services.nod.dans.knaw.nl:Products/dans:oai:easy.dans.knaw.nl:easy-dataset:101014 10|re3data_____::84e123776089ce3c7a33db98d9cd15a8 10|openaire____::9e3be59865b2c1c335d32dae2fe7b254 10|re3data_____::94816e6421eeb072e7742ce6a9decc5f 10|eurocrisdris::fe4903425d9040f680d8610d9079ea14 re3data_____::r3d100000044 10|openaire____::081b82f96300b6a6e3d282bad31cb6e2 10|opendoar____::8b6dd7db9af49e67306feb59a8bdc52c Life sciences medicine and health care protein evolution epistasis evolution of protein structure-function Meta II stability Cetacea spectral tuning Orcinus orca envir geo Dataset https://vocabularies.coar-repositories.org/resource_types/c_ddb1/ 2017 fttriple https://doi.org/10.5061/dryad.5k0s6 2023-01-22T17:08:26Z Like many aquatic vertebrates, whales have blue-shifting spectral tuning substitutions in the dim-light visual pigment, rhodopsin, that are thought to increase photosensitivity in underwater environments. We have discovered that known spectral tuning substitutions also have surprising epistatic effects on another function of rhodopsin, the kinetic rates associated with light-activated intermediates. By using absorbance spectroscopy and fluorescence-based retinal release assays on heterologously expressed rhodopsin, we assessed both spectral and kinetic differences between cetaceans (killer whale) and terrestrial outgroups (hippo, bovine). Mutation experiments revealed that killer whale rhodopsin is unusually resilient to pleiotropic effects on retinal release from key blue-shifting substitutions (D83N and A292S), largely due to a surprisingly specific epistatic interaction between D83N and the background residue, S299. Ancestral sequence reconstruction indicated that S299 is an ancestral residue that predates the evolution of blue-shifting substitutions at the origins of Cetacea. Based on these results, we hypothesize that intramolecular epistasis helped to conserve rhodopsin's kinetic properties while enabling blue-shifting spectral tuning substitutions as cetaceans adapted to aquatic environments. Trade-offs between different aspects of molecular function are rarely considered in protein evolution, but in cetacean and other vertebrate rhodopsins, may underlie multiple evolutionary scenarios for the selection of specific amino acid substitutions. Data for Dungan & Chang 2017, Proceedings BThe .zip archive contains two files: 1) A fasta alignment of the rhodopsin coding sequences used for ancestral sequence reconstruction and 2) an excel file with fluorescence and absorbance data seriesDunganChang2017_ProcB_Data.zip Dataset Killer Whale Orca Orcinus orca Killer whale Unknown |
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Unknown |
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language |
unknown |
topic |
Life sciences medicine and health care protein evolution epistasis evolution of protein structure-function Meta II stability Cetacea spectral tuning Orcinus orca envir geo |
spellingShingle |
Life sciences medicine and health care protein evolution epistasis evolution of protein structure-function Meta II stability Cetacea spectral tuning Orcinus orca envir geo Dungan, Sarah Z. Chang, Belinda S. W. Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin |
topic_facet |
Life sciences medicine and health care protein evolution epistasis evolution of protein structure-function Meta II stability Cetacea spectral tuning Orcinus orca envir geo |
description |
Like many aquatic vertebrates, whales have blue-shifting spectral tuning substitutions in the dim-light visual pigment, rhodopsin, that are thought to increase photosensitivity in underwater environments. We have discovered that known spectral tuning substitutions also have surprising epistatic effects on another function of rhodopsin, the kinetic rates associated with light-activated intermediates. By using absorbance spectroscopy and fluorescence-based retinal release assays on heterologously expressed rhodopsin, we assessed both spectral and kinetic differences between cetaceans (killer whale) and terrestrial outgroups (hippo, bovine). Mutation experiments revealed that killer whale rhodopsin is unusually resilient to pleiotropic effects on retinal release from key blue-shifting substitutions (D83N and A292S), largely due to a surprisingly specific epistatic interaction between D83N and the background residue, S299. Ancestral sequence reconstruction indicated that S299 is an ancestral residue that predates the evolution of blue-shifting substitutions at the origins of Cetacea. Based on these results, we hypothesize that intramolecular epistasis helped to conserve rhodopsin's kinetic properties while enabling blue-shifting spectral tuning substitutions as cetaceans adapted to aquatic environments. Trade-offs between different aspects of molecular function are rarely considered in protein evolution, but in cetacean and other vertebrate rhodopsins, may underlie multiple evolutionary scenarios for the selection of specific amino acid substitutions. Data for Dungan & Chang 2017, Proceedings BThe .zip archive contains two files: 1) A fasta alignment of the rhodopsin coding sequences used for ancestral sequence reconstruction and 2) an excel file with fluorescence and absorbance data seriesDunganChang2017_ProcB_Data.zip |
format |
Dataset |
author |
Dungan, Sarah Z. Chang, Belinda S. W. |
author_facet |
Dungan, Sarah Z. Chang, Belinda S. W. |
author_sort |
Dungan, Sarah Z. |
title |
Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin |
title_short |
Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin |
title_full |
Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin |
title_fullStr |
Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin |
title_full_unstemmed |
Data from: Epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin |
title_sort |
data from: epistatic interactions influence terrestrial-marine functional shifts in cetacean rhodopsin |
publisher |
Data Archiving and Networked Services (DANS) |
publishDate |
2017 |
url |
https://doi.org/10.5061/dryad.5k0s6 |
genre |
Killer Whale Orca Orcinus orca Killer whale |
genre_facet |
Killer Whale Orca Orcinus orca Killer whale |
op_source |
oai:easy.dans.knaw.nl:easy-dataset:101014 10.5061/dryad.5k0s6 oai:services.nod.dans.knaw.nl:Products/dans:oai:easy.dans.knaw.nl:easy-dataset:101014 10|re3data_____::84e123776089ce3c7a33db98d9cd15a8 10|openaire____::9e3be59865b2c1c335d32dae2fe7b254 10|re3data_____::94816e6421eeb072e7742ce6a9decc5f 10|eurocrisdris::fe4903425d9040f680d8610d9079ea14 re3data_____::r3d100000044 10|openaire____::081b82f96300b6a6e3d282bad31cb6e2 10|opendoar____::8b6dd7db9af49e67306feb59a8bdc52c |
op_relation |
http://dx.doi.org/10.5061/dryad.5k0s6 https://dx.doi.org/10.5061/dryad.5k0s6 |
op_rights |
lic_creative-commons |
op_doi |
https://doi.org/10.5061/dryad.5k0s6 |
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1766057433286836224 |