Affirmation of Distinctive Ribosomal Protein Paralog-Specific Ribosomes
34 Pages Posted: 15 Feb 2019 Publication Status: Review CompleteMore...
Accumulating evidences favor the existence of heterogeneous cellular ribosomes for versatile regulation of gene expression. Validation of distinctive ribosomal protein paralog-specific ribosomes in single cells at the protein level in nearly wild type background is essential for detailed understanding regarding the properties and functions of specialized ribosomes. Here we present results from cleanly purified RPL36 paralog-specific translating ribosomes to demonstrate they represent two distinctive populations characterized by specifically-enriched components. Under amino acid starvation, there is a dramatic reorganization in the composition of the two paralog-specific ribosomes together with reciprocal redistribution of the general translational factors and altered translational preference. pADH1-RPL36A manipulation improves the relative incompetency of the RPL36A gene; alters composition of both RPL36 paralog-specific ribosomes; reprograms genome-wide translational profile; and modifies the cellular ability to adapt to stress conditions while still preserving the paralog-specifically enriched components. Distinct folding is suggested to underlie functional differences between the paralogs.
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