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Molecular basis for protection of ribosomal protein L4 from cellular degradation
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Molecular basis for protection of ribosomal protein L4 from cellular degradation
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Journal Article
Molecular basis for protection of ribosomal protein L4 from cellular degradation
2017
Overview
Eukaryotic ribosome biogenesis requires the nuclear import of ∼80 nascent ribosomal proteins and the elimination of excess amounts by the cellular degradation machinery. Assembly chaperones recognize nascent unassembled ribosomal proteins and transport them together with karyopherins to their nuclear destination. We report the crystal structure of ribosomal protein L4 (RpL4) bound to its dedicated assembly chaperone of L4 (Acl4), revealing extensive interactions sequestering 70 exposed residues of the extended RpL4 loop. The observed molecular recognition fundamentally differs from canonical promiscuous chaperone–substrate interactions. We demonstrate that the eukaryote-specific RpL4 extension harbours overlapping binding sites for Acl4 and the nuclear transport factor Kap104, facilitating its continuous protection from the cellular degradation machinery. Thus, Acl4 serves a dual function to facilitate nuclear import and simultaneously protect unassembled RpL4 from the cellular degradation machinery.
Acl4 is a dedicated assembly chaperone for ribosomal protein RpL4 that recognizes RpL4 in the cytoplasm to facilitate its nuclear import. Here the authors reveal the mechanism whereby Acl4 recognizes RpL4 and functions to protect it from Tom1-mediated degradation until RpL4 incorporation into the maturing 60S pre-ribosomal subunit.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/535
/ Active Transport, Cell Nucleus
/ beta Karyopherins - chemistry
/ beta Karyopherins - metabolism
/ Humanities and Social Sciences
/ Molecular Chaperones - chemistry
/ Molecular Chaperones - metabolism
/ Peptides
/ Proteins
/ Ribosomal Proteins - chemistry
/ Ribosomal Proteins - metabolism
/ RNA
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - chemistry
/ Saccharomyces cerevisiae Proteins - metabolism
/ Science
/ Science & Technology - Other Topics
/ Yeast
