Proteomic Analysis of Ribosomes: Translational Control of mRNA Populations by Glycogen Synthase GYS1
| Autor: | Lori A. Kohlstaedt, Gabriele Fuchs, Camille Diges, Karen A. Wehner, Peter Sarnow |
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| Rok vydání: | 2011 |
| Předmět: |
Ribosomal Proteins
Blotting Western Biology Ribosome Article Structural Biology Ribosomal protein Polysome Protein biosynthesis Humans RNA Messenger RNA Small Interfering Glycogen synthase Molecular Biology Oligonucleotide Array Sequence Analysis Reverse Transcriptase Polymerase Chain Reaction Eukaryotic Large Ribosomal Subunit Gene Expression Profiling Translation (biology) Blotting Northern Glycogen Synthase Biochemistry Polyribosomes Protein Biosynthesis Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Eukaryotic Ribosome Ribosomes Biomarkers HeLa Cells |
| Zdroj: | Journal of Molecular Biology. 410:118-130 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2011.04.064 |
| Popis: | Ribosomes exist as a heterogenous pool of macromolecular complexes composed of ribosomal RNA molecules, ribosomal proteins, and numerous associated "nonribosomal" proteins. To identify nonribosomal proteins that may modulate ribosome activity, we examined the composition of translationally active and inactive ribosomes using a proteomic multidimensional protein identification technology. Notably, the phosphorylated isoform of glycogen synthase, glycogen synthase 1 (GYS1), was preferentially associated with elongating ribosomes. Depletion of GYS1 affected the translation of a subset of cellular mRNAs, some of which encode proteins that modulate protein biosynthesis. These findings argue that GYS1 abundance, by virtue of its ribosomal association, provides a feedback loop between the energy state of the cells and the translation machinery. |
| Databáze: | OpenAIRE |
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