Halophilic to mesophilic adaptation of ubiquitin-like proteins.
FEBS Lett
; 595(4): 521-531, 2021 02.
Article
en En
| MEDLINE
| ID: mdl-33301612
ABSTRACT
Elucidating how proteins adapt from halophilic to mesophilic environments will enable a better understanding of protein evolution and folding. In this study, by directed evolution and site-directed mutagenesis of the halophilic ubiquitin-like protein (ULP) Samp2, we find that substitution of the prebiotic amino acid Asp31 by Gly is uniquely effective in the mesophilic adaptation of ULP. Sequence analysis shows that substitution of Asp/Glu in halophilic ULPs by Gly in mesophilic ULPs has higher occurrence than other substitutions, supporting the unique role of the substitution in the mesophilic adaptation of ULP. Molecular dynamic simulations indicate that the mesophilic adaptation might result from the effect of the substitution on the conformational flexibility of ULP.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Contexto en salud:
3_ND
Problema de salud:
3_neglected_diseases
/
3_zoonosis
Asunto principal:
Cloruro de Sodio
/
Ubiquitinas
/
Pliegue de Proteína
/
Cloruro de Cadmio
/
Haloferax volcanii
/
Proteínas Arqueales
Límite:
Animals
Idioma:
En
Revista:
FEBS Lett
Año:
2021
Tipo del documento:
Article
País de afiliación:
China