PUBLICATION

Birth of a pathway for sulfur metabolism in early amniote evolution

Authors
Malatesta, M., Mori, G., Acquotti, D., Campanini, B., Peracchi, A., Antin, P.B., Percudani, R.
ID
ZDB-PUB-220103-1
Date
2020
Source
Nature ecology & evolution   4: 1239-1246 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Sulfur
  • Cystathionine beta-Synthase/genetics
  • Hydrogen Sulfide*
  • Chick Embryo
  • Cystathionine gamma-Lyase*
  • Cysteine
  • Animals
PubMed
32601391 Full text @ Nat Ecol Evol
Abstract
Among amniotes, reptiles and mammals are differently adapted to terrestrial life. It is generally appreciated that terrestrialization required adaptive changes of vertebrate metabolism, particularly in the mode of nitrogen excretion. However, the current paradigm is that metabolic adaptation to life on land did not involve synthesis of enzymatic pathways de novo, but rather repurposing of existing ones. Here, by comparing the inventory of pyridoxal 5'-phosphate-dependent enzymes in different amniotes, we identify in silico a pathway for sulfur metabolism present in chick embryos but not in mammals. Cysteine lyase contains haem and pyridoxal 5'-phosphate co-factors and converts cysteine and sulfite into cysteic acid and hydrogen sulfide, respectively. A specific cysteic acid decarboxylase produces taurine, while hydrogen sulfide is recycled into cysteine by cystathionine beta-synthase. This reaction sequence enables the formation of sulfonated amino acids during embryo development in the egg at no cost of reduced sulfur. The pathway originated around 300 million years ago in a proto-reptile by cystathionine beta-synthase duplication, cysteine lyase neofunctionalization and cysteic acid decarboxylase co-option. Our findings indicate that adaptation to terrestrial life involved innovations in metabolic pathways, and reveal the molecular mechanisms by which such innovations arose in amniote evolution.
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