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MS data for Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis

ABSTRACT: Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. It is not clear how this promiscuous mechanism ensure efficient production of challenging clients such as highly expressed proteins. Here we find that the biogenesis of the abundantly expressed eukaryotic translation elongation factor 1A (eEF1A) depends on the dedicated ribosome-associated chaperone Chp1.

INSTRUMENT(S): Thermo Finnigan instrument model

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Jany Quintana Cordero

LAB HEAD: Claes Andréasson

PROVIDER: PXD043391 | Pride | 2024-06-16

REPOSITORIES: Pride

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Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis.

Minoia Melania M Quintana-Cordero Jany J Jetzinger Katharina K Kotan Ilgin Eser IE Turnbull Kathryn Jane KJ Ciccarelli Michela M Masser Anna E AE Liebers Dorina D Gouarin Eloïse E Czech Marius M Hauryliuk Vasili V Bukau Bernd B Kramer Günter G Andréasson Claes C

Nature communications 20240215 1

Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated chaperone, Chp1, that rewires the cotranslational folding machinery to assist in the challenging biogenesis of abundantly expressed eukaryotic translation elongation factor 1A (eEF1A). Our results indicate that during eEF1A synthesis, Chp1 is recruited to the ribosome with the help of the nascent polypeptide-associated complex ...[more]

PMID: 38360885

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