Unknown

Dataset Information

0

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 ?-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.

SUBMITTER: Pausch P 

PROVIDER: S-EPMC4491177 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

altmetric image

Publications

Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.

Pausch Patrick P   Singh Ujjwala U   Ahmed Yasar Luqman YL   Pillet Benjamin B   Murat Guillaume G   Altegoer Florian F   Stier Gunter G   Thoms Matthias M   Hurt Ed E   Sinning Irmgard I   Bange Gert G   Kressler Dieter D  

Nature communications 20150626


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 dedicate  ...[more]

Similar Datasets

| S-EPMC8970588 | biostudies-literature
| S-EPMC10256725 | biostudies-literature
| S-EPMC7551657 | biostudies-literature
| S-EPMC2934618 | biostudies-literature
| S-EPMC8627912 | biostudies-literature
| S-EPMC6928942 | biostudies-literature
| PRJEB53855 | ENA
| S-EPMC10191850 | biostudies-literature
| S-EPMC9197937 | biostudies-literature
| S-EPMC3870195 | biostudies-literature