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How Does the Ribosome Fold the Proteome?
Cassaignau, Anaïs M E; Cabrita, Lisa D; Christodoulou, John.
Afiliación
  • Cassaignau AME; Institute of Structural and Molecular Biology, University College London and Birkbeck College, London WC1E 7HX, United Kingdom; email: anais.cassaignau.09@ucl.ac.uk, l.cabrita@ucl.ac.uk, j.christodoulou@ucl.ac.uk.
  • Cabrita LD; Institute of Structural and Molecular Biology, University College London and Birkbeck College, London WC1E 7HX, United Kingdom; email: anais.cassaignau.09@ucl.ac.uk, l.cabrita@ucl.ac.uk, j.christodoulou@ucl.ac.uk.
  • Christodoulou J; Institute of Structural and Molecular Biology, University College London and Birkbeck College, London WC1E 7HX, United Kingdom; email: anais.cassaignau.09@ucl.ac.uk, l.cabrita@ucl.ac.uk, j.christodoulou@ucl.ac.uk.
Annu Rev Biochem ; 89: 389-415, 2020 06 20.
Article en En | MEDLINE | ID: mdl-32569518
Folding of polypeptides begins during their synthesis on ribosomes. This process has evolved as a means for the cell to maintain proteostasis, by mitigating the risk of protein misfolding and aggregation. The capacity to now depict this cellular feat at increasingly higher resolution is providing insight into the mechanistic determinants that promote successful folding. Emerging from these studies is the intimate interplay between protein translation and folding, and within this the ribosome particle is the key player. Its unique structural properties provide a specialized scaffold against which nascent polypeptides can begin to form structure in a highly coordinated, co-translational manner. Here, we examine how, as a macromolecular machine, the ribosome modulates the intrinsic dynamic properties of emerging nascent polypeptide chains and guides them toward their biologically active structures.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Ribosomas / Biosíntesis de Proteínas / Chaperonas Moleculares / Proteoma / Escherichia coli Límite: Humans Idioma: En Revista: Annu Rev Biochem Año: 2020 Tipo del documento: Article

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Ribosomas / Biosíntesis de Proteínas / Chaperonas Moleculares / Proteoma / Escherichia coli Límite: Humans Idioma: En Revista: Annu Rev Biochem Año: 2020 Tipo del documento: Article