Precise Post-translational Tuning Occurs for Most Protein Complex Components during Meiosis.
Protein degradation is known to be a key component of expression regulation for individual genes, but its global impact on gene expression has been difficult to determine. We analyzed a parallel gene expression dataset of yeast meiotic differentiation, identifying instances of coordinated protein-level decreases to identify new cases of regulated meiotic protein degradation, including of ribosomes and targets of the meiosis-specific anaphase-promoting complex adaptor Ama1. Comparison of protein and translation measurements over time also revealed that, although meiotic cells are capable of synthesizing protein complex members at precisely matched levels, they typically do not. Instead, the members of most protein complexes are synthesized imprecisely, but their protein levels are matched, indicating that wild-type eukaryotic cells routinely use post-translational adjustment of protein complex partner levels to achieve proper stoichiometry. Outlier cases, in which specific complex components show divergent protein-level trends, suggest timed regulation of these complexes.
['Eisenberg|Amy Rose|AR|', 'Higdon|Andrea|A|', 'Keskin|Abdurrahman|A|', 'Hodapp|Stefanie|S|', 'Jovanovic|Marko|M|', 'Brar|Gloria Ann|GA|']
D015966:Gene Expression Regulation, Fungal D008540:Meiosis D046912:Multiprotein Complexes D011485:Protein Binding D014176:Protein Biosynthesis D055503:Protein Multimerization D011499:Protein Processing, Post-Translational D059748:Proteolysis D012269:Ribosomal Proteins D012441:Saccharomyces cerevisiae D029701:Saccharomyces cerevisiae Proteins
protein complexes meiosis protein degradation gene expression ribosome Ama1 translation stoichiometry mass spectrometry ribosome profiling