Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly.
Nucleic Acids Res
; 50(16): 9490-9504, 2022 09 09.
Article
en En
| MEDLINE
| ID: mdl-35971611
Protein synthesis in eukaryotic cell is spatially and structurally compartmentalized that ensures high efficiency of this process. One of the distinctive features of higher eukaryotes is the existence of stable multi-protein complexes of aminoacyl-tRNA synthetases and translation elongation factors. Here, we report a quaternary organization of the human guanine-nucleotide exchange factor (GEF) complex, eEF1B, comprising α, ß and γ subunits that specifically associate into a heterotrimeric form eEF1B(αßγ)3. As both the eEF1Bα and eEF1Bß proteins have structurally conserved GEF domains, their total number within the complex is equal to six. Such, so far, unique structural assembly of the guanine-nucleotide exchange factors within a stable complex may be considered as a 'GEF hub' that ensures efficient maintenance of the translationally active GTP-bound conformation of eEF1A in higher eukaryotes.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Factor 1 de Elongación Peptídica
/
Factores de Intercambio de Guanina Nucleótido
Límite:
Humans
Idioma:
En
Revista:
Nucleic Acids Res
Año:
2022
Tipo del documento:
Article
País de afiliación:
Ucrania
Pais de publicación:
Reino Unido