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Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly.
Bondarchuk, Tetiana V; Shalak, Vyacheslav F; Lozhko, Dmytro M; Fatalska, Agnieszka; Szczepanowski, Roman H; Liudkovska, Vladyslava; Tsuvariev, Oleksandr Yu; Dadlez, Michal; El'skaya, Anna V; Negrutskii, Boris S.
Afiliación
  • Bondarchuk TV; Institute of Molecular Biology and Genetics, NAS of Ukraine, 150 Zabolotnogo St., 03143 Kyiv, Ukraine.
  • Shalak VF; Institute of Molecular Biology and Genetics, NAS of Ukraine, 150 Zabolotnogo St., 03143 Kyiv, Ukraine.
  • Lozhko DM; Institute of Molecular Biology and Genetics, NAS of Ukraine, 150 Zabolotnogo St., 03143 Kyiv, Ukraine.
  • Fatalska A; Institute of Biochemistry and Biophysics, PAN, Pawinskiego 5a, 02-109 Warsaw, Poland.
  • Szczepanowski RH; Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK.
  • Liudkovska V; International Institute of Molecular and Cell Biology, Trojdena 4, 02-109 Warsaw, Poland.
  • Tsuvariev OY; Institute of Molecular Biology and Genetics, NAS of Ukraine, 150 Zabolotnogo St., 03143 Kyiv, Ukraine.
  • Dadlez M; International Institute of Molecular and Cell Biology, Trojdena 4, 02-109 Warsaw, Poland.
  • El'skaya AV; Institute of High Technologies, Taras Shevchenko National University of Kyiv, Akademik Glushkov Ave. 4-g, 03022 Kyiv, Ukraine.
  • Negrutskii BS; Institute of Biochemistry and Biophysics, PAN, Pawinskiego 5a, 02-109 Warsaw, Poland.
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.
Asunto(s)

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

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