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Originally published In Press as doi:10.1074/mcp.M800051-MCP200 on May 2, 2008.
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Molecular & Cellular Proteomics 7:1530-1540, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.


Research

Comprehensive Analysis of the Effects of Escherichia coli ORFs on Protein Translation Reaction*,S

Yasuaki Kazuta{ddagger},§, Jiro Adachi{ddagger},§, Tomoaki Matsuura{ddagger},§, Naoaki Ono{ddagger}, Hirotada Mori,|| and Tetsuya Yomo{ddagger},**,{ddagger}{ddagger},§§

From the {ddagger} Department of Bioinformatics Engineering, {ddagger}{ddagger} Graduate School of Information Science and Technology, Osaka University and ** Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Agency (JST), 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan, Institute for Advanced Biosciences, Keio University, 14-1 Baba-cho, Tsuruoka City, Yamagata, 997-0035, Japan, || Graduate School of Biological Sciences, and Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0192, Japan

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.


§§ To whom correspondence should be addressed: Dept. of Bioinformatics Engineering, Graduate School of Information Science and Technology, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-4171; Fax: 81-6-6879-7428; E-mail: yomo{at}ist.osaka-u.ac.jp


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