Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.
Abstract
Exponentially growing yeast cells produce every minute >160,000 ribosomal proteins. Owing to their difficult physicochemical properties, the synthesis of assembly-competent ribosomal proteins represents a major challenge. Recent evidence highlights that dedicated chaperone proteins recognize the N-terminal regions of ribosomal proteins and promote their soluble expression and delivery to the assembly site. Here we explore the intuitive possibility that ribosomal proteins are captured by dedicated chaperones in a co-translational manner. Affinity purification of four chaperones (Rrb1, Syo1, Sqt1 and Yar1) selectively enriched the mRNAs encoding their specific ribosomal protein clients (Rpl3, Rpl5, Rpl10 and Rps3). X-ray crystallography reveals how the N-terminal, rRNA-binding residues of Rpl10 are shielded by Sqt1's WD-repeat β-propeller, providing mechanistic insight into the incorporation of Rpl10 into pre-60S subunits. Co-translational capturing of nascent ribosomal proteins by dedicated chaperones constitutes an elegant mechanism to prevent unspecific interactions and aggregation of ribosomal proteins on their road to incorporation.
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BibTeX
@article{pausch2026cotranslational,
title = {{Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.}},
author = {Pausch P and Singh U and Ahmed Yl and Pillet B and Murat G and Altegoer F and Stier G and Thoms M and Hurt E and Sinning I and Bange G and Kressler D},
journal = {Nature Communications},
year = {2026},
month = oct,
doi = {10.1038/ncomms8494},
url = {https://hal.science/hal-05780546v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.
AU - Pausch P
AU - Singh U
AU - Ahmed Yl
AU - Pillet B
AU - Murat G
AU - Altegoer F
AU - Stier G
AU - Thoms M
AU - Hurt E
AU - Sinning I
AU - Bange G
AU - Kressler D
PY - 2026
DA - 2026/10/06
JO - Nature Communications
DO - 10.1038/ncomms8494
UR - https://hal.science/hal-05780546v1
AB - Exponentially growing yeast cells produce every minute >160,000 ribosomal proteins. Owing to their difficult physicochemical properties, the synthesis of assembly-competent ribosomal proteins represents a major challenge. Recent evidence highlights that dedicated chaperone proteins recognize the N-terminal regions of ribosomal proteins and promote their soluble expression and delivery to the assembly site. Here we explore the intuitive possibility that ribosomal proteins are captured by dedicated chaperones in a co-translational manner. Affinity purification of four chaperones (Rrb1, Syo1, Sqt1 and Yar1) selectively enriched the mRNAs encoding their specific ribosomal protein clients (Rpl3, Rpl5, Rpl10 and Rps3). X-ray crystallography reveals how the N-terminal, rRNA-binding residues of Rpl10 are shielded by Sqt1's WD-repeat β-propeller, providing mechanistic insight into the incorporation of Rpl10 into pre-60S subunits. Co-translational capturing of nascent ribosomal proteins by dedicated chaperones constitutes an elegant mechanism to prevent unspecific interactions and aggregation of ribosomal proteins on their road to incorporation.
SN - 2041-1723
SN - 2041-1723
ER -