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PDBsum entry 4zox
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References listed in PDB file
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Key reference
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Title
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Co-Translational capturing of nascent ribosomal proteins by their dedicated chaperones.
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Authors
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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.
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Ref.
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Nat Commun, 2015,
6,
7494.
[DOI no: ]
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PubMed id
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Abstract
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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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