Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding
Metadatos
Mostrar el registro completo del ítemAutor
Gámiz Arco, María Gloria; Risso, Valeria Alejandra; Candel, Adela M.; Inglés Prieto, Álvaro; Romero Romero, María Luisa; Gaucher, Eric A.; Gavira Gallardo, José Antonio; Ibarra Molero, Beatriz; Sánchez Ruiz, José ManuelEditorial
Portland Press
Fecha
2019Referencia bibliográfica
Gamiz-Arco, G., Risso, V. A., Candel, A. M., Inglés-Prieto, A., Romero-Romero, M. L., Gaucher, E. A., ... & Sanchez-Ruiz, J. M. (2019). Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding. Biochemical Journal, 476(23), 3631-3647.
Patrocinador
This research was supported by FEDER Funds, grant BIO2015-66426-R from the Spanish Ministry of Economy and Competitiveness ( J.M.S.-R.), grant RGP0041/2017 from the Human Frontier Science Program ( J.M.S.-R. and E.A.G.) and National Institutes of Health 1R01AR069137 (E.A.G.), Department of Defence MURI W911NF-16-1-0372 (E.A.G.).Resumen
Evolution involves not only adaptation, but also the degradation of superfluous features.
Many examples of degradation at the morphological level are known (vestigial organs, for
instance). However, the impact of degradation on molecular evolution has been rarely
addressed. Thioredoxins serve as general oxidoreductases in all cells. Here, we report
extensive mutational analyses on the folding of modern and resurrected ancestral bacterial
thioredoxins. Contrary to claims from recent literature, in vitro folding rates in the thioredoxin
family are not evolutionarily conserved, but span at least a ∼100-fold range.
Furthermore, modern thioredoxin folding is often substantially slower than ancestral thioredoxin
folding. Unassisted folding, as probed in vitro, thus emerges as an ancestral vestigial
feature that underwent degradation, plausibly upon the evolutionary emergence of
efficient cellular folding assistance. More generally, our results provide evidence that degradation
of ancestral features shapes, not only morphological evolution, but also the evolution
of individual proteins.