| Título: | Protein disulfide oxidoreductases and the evolution of thermophily: was the last common ancestor a heatloving microbe? |
| Autores: |
Becerra Bracho, Arturo Carlos ll Delaye, L Lazcano Araujo Reyes, Antonio Eusebio Orgel, L |
| Fecha: |
20130312T14:38:32Z 20130312T14:38:32Z 2007 |
| Publicador: | Facultad de Ciencias - UNAM |
| Fuente: |
 |
| Tipo: | Artículo de investigación |
| Tema: |
Biochemistry & Molecular Biology Evolutionary Biology Genetics & Heredity protein disulfide oxidoreductases thermophily last common ancestor horizontal gene transfer |
| Descripción: | Protein disulfide oxidoreductases (PDOs) are redox enzymes that catalyze dithioldisulfide exchange reactions. Their sequences and structure reveal the presence of two thioredoxin fold units, each of which is endowed with a catalytic site CXXC motif. PDOs are the outcome of an ancient gene duplication event. They have been described in a number of thermophilic and hyperthermophilic species, where they play a critical role in the structural stabilization of intracellular proteins. PDOs are homologous to both the Nterminal domain of the bacterial alkyl hydroperoxide reductase (AhpF) and to the eukaryotic protein disulfide isomerase (PDI). Phylogenetic analysis of PDOs suggests that they first evolved in the crenarchaeota, spreading freom them into the Bacteria via the euryarchaeota. These results imply that the last common ancestor (LCA) of all extant living beings lacked a PDO and argue, albeit weakly, against a thermophilic LCA. |
| Idioma: | Inglés |