Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: White LJ 

PROVIDER: S-EPMC7657897 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

White Lewis J LJ   Sutton Gemma G   Shechonge Asilatu A   Day Julia J JJ   Dasmahapatra Kanchon K KK   Pownall Mary E ME  

Royal Society open science 20201014 10


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 <i>Oreochromis Alcolapia</i>, 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 <i>Alcolapia</i> is  ...[more]

Similar Datasets

| S-EPMC2280008 | biostudies-literature
| S-EPMC2286696 | biostudies-literature
| S-EPMC6817081 | biostudies-literature
| S-EPMC2698666 | biostudies-literature
| S-EPMC2847351 | biostudies-literature
| S-EPMC3944931 | biostudies-literature
| S-EPMC24219 | biostudies-literature
| S-EPMC3359619 | biostudies-literature
| S-EPMC1168186 | biostudies-other
| S-EPMC8604956 | biostudies-literature