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4ZOX

Crystal structure of the Saccharomyces cerevisiae Sqt1 bound to the N-terminus of the ribosomal protein L10

Summary for 4ZOX
Entry DOI10.2210/pdb4zox/pdb
Related4ZOV
DescriptorRibosome assembly protein SQT1, 60S ribosomal protein L10 (3 entities in total)
Functional Keywordschaperone, ribosomal biogenesis, wd40 - repeat
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Cellular locationCytoplasm : P41805
Total number of polymer chains2
Total formula weight44902.74
Authors
Pausch, P.,Altegoer, F.,Bange, G. (deposition date: 2015-05-07, release date: 2015-07-01, Last modification date: 2024-01-10)
Primary citationPausch, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2025-06-11公开中

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