PDBsum entry 4zox

Chaperone

PDB id: 4zox

Contents

Protein chains

379 a.a.

14 a.a.

Waters ×559

PDB id:

4zox

Name:

Chaperone

Title:

Crystal structure of the saccharomyces cerevisiae sqt1 bound to the n- terminus of the ribosomal protein l10

Structure:

Ribosome assembly protein sqt1. Chain: a. Fragment: unp residues 53-431. Engineered: yes. 60s ribosomal protein l10. Chain: b. Fragment: unp residues 1-20. Synonym: rpl10, l9,ubiquinol-cytochromE C reductase complex subunit vi-requiring protein.

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: sqt1, yir012w, yib12w. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: rpl10, grc5, qsr1, ylr075w. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.148 R-free: 0.181

Authors:

P.Pausch,F.Altegoer,G.Bange

Key ref:

P.Pausch et al. (2015). Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones. Nat Commun, 6, 7494. PubMed id: 26112308 DOI: 10.1038/ncomms8494

Date:

07-May-15 Release date: 01-Jul-15

Protein chain

P35184  (SQT1_YEAST) -  Ribosome assembly protein SQT1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 431 a.a.

Struc: 379 a.a.

Protein chain

P41805  (RL10_YEAST) -  Large ribosomal subunit protein uL16 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 221 a.a.

Struc: 14 a.a.

DOI no: 10.1038/ncomms8494

Nat Commun 6:7494 (2015)

PubMed id: 26112308

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

P.Pausch, U.Singh, Y.L.Ahmed, B.Pillet, G.Murat, F.Altegoer, G.Stier, M.Thoms, E.Hurt, I.Sinning, G.Bange, D.Kressler.

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.