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Cotranslational sorting and processing of newly synthesized proteins in eukaryotes.
Gamerdinger, Martin; Deuerling, Elke.
Afiliación
  • Gamerdinger M; Department of Biology, Molecular Microbiology, University of Konstanz, 78457 Konstanz, Germany. Electronic address: martin.gamerdinger@uni-konstanz.de.
  • Deuerling E; Department of Biology, Molecular Microbiology, University of Konstanz, 78457 Konstanz, Germany. Electronic address: elke.deuerling@uni-konstanz.de.
Trends Biochem Sci ; 49(2): 105-118, 2024 02.
Article en En | MEDLINE | ID: mdl-37919225
ABSTRACT
Ribosomes interact with a variety of different protein biogenesis factors that guide newly synthesized proteins to their native 3D shapes and cellular localization. Depending on the type of translated substrate, a distinct set of cotranslational factors must interact with the ribosome in a timely and coordinated manner to ensure proper protein biogenesis. While cytonuclear proteins require cotranslational maturation and folding factors, secretory proteins must be maintained in an unfolded state and processed cotranslationally by transport and membrane translocation factors. Here we explore the specific cotranslational processing steps for cytonuclear, secretory, and membrane proteins in eukaryotes and then discuss how the nascent polypeptide-associated complex (NAC) cotranslationally sorts these proteins into the correct protein biogenesis pathway.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Ribosomas / Biosíntesis de Proteínas Idioma: En Revista: Trends Biochem Sci Año: 2024 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Ribosomas / Biosíntesis de Proteínas Idioma: En Revista: Trends Biochem Sci Año: 2024 Tipo del documento: Article