Cargando…
Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding
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 gen...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6906118/ https://www.ncbi.nlm.nih.gov/pubmed/31750876 http://dx.doi.org/10.1042/BCJ20190739 |
_version_ | 1783478287306063872 |
---|---|
author | Gamiz-Arco, Gloria Risso, Valeria A. Candel, Adela M. Inglés-Prieto, Alvaro Romero-Romero, Maria L. Gaucher, Eric A. Gavira, Jose A. Ibarra-Molero, Beatriz Sanchez-Ruiz, Jose M. |
author_facet | Gamiz-Arco, Gloria Risso, Valeria A. Candel, Adela M. Inglés-Prieto, Alvaro Romero-Romero, Maria L. Gaucher, Eric A. Gavira, Jose A. Ibarra-Molero, Beatriz Sanchez-Ruiz, Jose M. |
author_sort | Gamiz-Arco, Gloria |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6906118 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-69061182019-12-16 Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding Gamiz-Arco, Gloria Risso, Valeria A. Candel, Adela M. Inglés-Prieto, Alvaro Romero-Romero, Maria L. Gaucher, Eric A. Gavira, Jose A. Ibarra-Molero, Beatriz Sanchez-Ruiz, Jose M. Biochem J Biophysics 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. Portland Press Ltd. 2019-12-12 2019-12-10 /pmc/articles/PMC6906118/ /pubmed/31750876 http://dx.doi.org/10.1042/BCJ20190739 Text en © 2019 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Biophysics Gamiz-Arco, Gloria Risso, Valeria A. Candel, Adela M. Inglés-Prieto, Alvaro Romero-Romero, Maria L. Gaucher, Eric A. Gavira, Jose A. Ibarra-Molero, Beatriz Sanchez-Ruiz, Jose M. Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding |
title | Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding |
title_full | Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding |
title_fullStr | Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding |
title_full_unstemmed | Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding |
title_short | Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding |
title_sort | non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding |
topic | Biophysics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6906118/ https://www.ncbi.nlm.nih.gov/pubmed/31750876 http://dx.doi.org/10.1042/BCJ20190739 |
work_keys_str_mv | AT gamizarcogloria nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT rissovaleriaa nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT candeladelam nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT inglesprietoalvaro nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT romeroromeromarial nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT gauchererica nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT gavirajosea nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT ibarramolerobeatriz nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding AT sanchezruizjosem nonconservationoffoldingratesinthethioredoxinfamilyrevealsdegradationofancestralunassistedfolding |