ArticleMolecular & cellular proteomics : MCP2008
Comprehensive analysis of the effects of Escherichia coli ORFs on protein translation reaction.
Article in Molecular & cellular proteomics : MCP, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The Long Road to a Synthetic Self-Replicating Central Dogma.Biochemistry · 2023Review
- In vitro synthesis of 32 translation-factor proteins from a single template reveals impaired ribosomal processivity.Scientific reports · 2021Article
- Bottom-Up Construction of Complex Biomolecular Systems With Cell-Free Synthetic Biology.Frontiers in bioengineering and biotechnology · 2020Review
- Self-replication of DNA by its encoded proteins in liposome-based synthetic cells.Nature communications · 2018Article
- De novo design and synthesis of a 30-cistron translation-factor module.Nucleic acids research · 2017Article
- Dissecting limiting factors of the Protein synthesis Using Recombinant Elements (PURE) system.Translation (Austin, Tex.) · 2017Article
- Evolutionary Consequence of a Trade-Off between Growth and Maintenance along with Ribosomal Damages.PloS one · 2015Article
- Liposome display for in vitro selection and evolution of membrane proteins.Nature protocols · 2014Article
- Global analysis of chaperone effects using a reconstituted cell-free translation system.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Kinetic analysis of β-galactosidase and β-glucuronidase tetramerization coupled with protein translation.The Journal of biological chemistry · 2011Article
- Evolution combined with genomic study elucidates genetic bases of isobutanol tolerance in Escherichia coli.Microbial cell factories · 2011Article
- Update on designing and building minimal cells.Current opinion in biotechnology · 2010Review
- Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Quantifying epistatic interactions among the components constituting the protein translation system.Molecular systems biology · 2009Article
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Authors and funding
6 authors.
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Abstract
Protein synthesis is one of the most important reactions in the cell. Recent experimental studies indicated that this complex reaction can be achieved with a minimum complement of 36 proteins and ribosomes by reconstituting an Escherichia coli-based in vitro translation system with these protein components highly purified on an individual basis. From the protein-protein interaction (PPI) network of E. coli proteins, these minimal protein components are known to interact physically with large numbers of proteins. However, it is unclear what fraction of E. coli proteins are linked functionally with the minimal protein synthesis system. We investigated the effects of each of the 4194 E. coli ORF products on the minimal protein synthesis system; at least 12% of the entire ORF products, a significant fraction of the gene product of E. coli, affect the activity of this system. Furthermore 34% of these functional modifiers present in the PPI network were shown by mapping to be directly linked (i.e. to interact physically) with the minimal components of the PPI network. Topological analysis of the relationships between modifiers and the minimal components in the PPI network indicated clustering of the minimal components. The modifiers showed no such clustering, indicating that the location of functional modifiers is spread across the PPI network rather than clustering close to the minimal protein components. These observations may reflect the evolutionary process of the protein synthesis system.
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