Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fish

Tetrapods and fish have adapted distinct carbamoyl-phosphate synthase (CPS) enzymes to initiate the ornithine urea cycle during the detoxification of nitrogenous wastes. We report evidence that in the ureotelic subgenus of extremophile fish Oreochromis Alcolapia, CPS III has undergone convergent evo...

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Main Authors: Lewis J. White, Gemma Sutton, Asilatu Shechonge, Julia J. Day, Kanchon K. Dasmahapatra, Mary E. Pownall
Format: Article
Language:English
Published: The Royal Society 2020-10-01
Series:Royal Society Open Science
Subjects:
Online Access:https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.201200
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author Lewis J. White
Gemma Sutton
Asilatu Shechonge
Julia J. Day
Kanchon K. Dasmahapatra
Mary E. Pownall
author_facet Lewis J. White
Gemma Sutton
Asilatu Shechonge
Julia J. Day
Kanchon K. Dasmahapatra
Mary E. Pownall
author_sort Lewis J. White
collection DOAJ
description Tetrapods and fish have adapted distinct carbamoyl-phosphate synthase (CPS) enzymes to initiate the ornithine urea cycle during the detoxification of nitrogenous wastes. We report evidence that in the ureotelic subgenus of extremophile fish Oreochromis Alcolapia, CPS III has undergone convergent evolution and adapted its substrate affinity to ammonia, which is typical of terrestrial vertebrate CPS I. Unusually, unlike in other vertebrates, the expression of CPS III in Alcolapia is localized to the skeletal muscle and is activated in the myogenic lineage during early embryonic development with expression remaining in mature fish. We propose that adaptation in Alcolapia included both convergent evolution of CPS function to that of terrestrial vertebrates, as well as changes in development mechanisms redirecting CPS III gene expression to the skeletal muscle.
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spelling doaj.art-aca69784068e419d9b7a9a0b85b9aaee2022-12-22T00:28:19ZengThe Royal SocietyRoyal Society Open Science2054-57032020-10-0171010.1098/rsos.201200201200Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fishLewis J. WhiteGemma SuttonAsilatu ShechongeJulia J. DayKanchon K. DasmahapatraMary E. PownallTetrapods and fish have adapted distinct carbamoyl-phosphate synthase (CPS) enzymes to initiate the ornithine urea cycle during the detoxification of nitrogenous wastes. We report evidence that in the ureotelic subgenus of extremophile fish Oreochromis Alcolapia, CPS III has undergone convergent evolution and adapted its substrate affinity to ammonia, which is typical of terrestrial vertebrate CPS I. Unusually, unlike in other vertebrates, the expression of CPS III in Alcolapia is localized to the skeletal muscle and is activated in the myogenic lineage during early embryonic development with expression remaining in mature fish. We propose that adaptation in Alcolapia included both convergent evolution of CPS function to that of terrestrial vertebrates, as well as changes in development mechanisms redirecting CPS III gene expression to the skeletal muscle.https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.201200ureacarbamoyl-phosphate synthetasealcolapiaextremophilefish
spellingShingle Lewis J. White
Gemma Sutton
Asilatu Shechonge
Julia J. Day
Kanchon K. Dasmahapatra
Mary E. Pownall
Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fish
Royal Society Open Science
urea
carbamoyl-phosphate synthetase
alcolapia
extremophile
fish
title Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fish
title_full Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fish
title_fullStr Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fish
title_full_unstemmed Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fish
title_short Adaptation of the carbamoyl-phosphate synthetase enzyme in an extremophile fish
title_sort adaptation of the carbamoyl phosphate synthetase enzyme in an extremophile fish
topic urea
carbamoyl-phosphate synthetase
alcolapia
extremophile
fish
url https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.201200
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