4ZN4

Crystal structure of Sqt1 from Chaetomium thermophilum solved by MR

Summary for 4ZN4

• Entry DOI: 10.2210/pdb4zn4/pdb
• Related: 4ZOV 4ZOX 4ZOY 4ZOZ
• Descriptor: sqt1, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ribosome biogenesis, chaperone
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• Total number of polymer chains: 2
• Total formula weight: 114347.26

Authors

Ahmed, Y.L.,Sinning, I. (deposition date: 2015-05-04, release date: 2015-07-01, Last modification date: 2024-01-10)

Primary citation

Pausch, P.,Singh, U.,Ahmed, Y.L.,Pillet, B.,Murat, G.,Altegoer, F.,Stier, G.,Thoms, M.,Hurt, E.,Sinning, I.,Bange, G.,Kressler, D.
Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.
Nat Commun, 6:7494-7494, 2015

PubMed 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.

PubMed: 26112308
DOI: 10.1038/ncomms8494

Experimental method

X-RAY DIFFRACTION (1.94 Å)