Detection of the Protein-Protein Interaction between Cyclic AMP Receptor Protein and RNA Polymerase, by 13C-Carbonyl NMR.
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概要
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Cyclic AMP receptor protein (CRP) plays a key role in the transcription regulation of many prokaryotic genes. Upon the binding of cyclic Am-P, CRP is allosterically activated, binds to target DNA sites, and interacts with RNA polymerase. Although the protein-protein interaction between CRP and RNA polymerase is known to be important for the transcription initiation of the target genes, its structural understanding is still lacking, particularly due to the high molecular mass (_??_120 kDa) of the protein complex. We assigned all of the 13C-carbonyl resonances of methionine residues in CRP by using the double labeling and the enzyme digestion techniques. The result of 13C-carbonyl NMR experiment on [13C'-Met]-CRP in the presence of both cyclic AMP and RNA polymerase a subunit showed that the two proteins interact with each other in solution in the absence of DNA via the region around the residues from Met 157 to Met 163 in CRP. The results also showed the effectiveness of the selective labeling and 13C-carbonyl NMR spectroscopy in the specific detection of the protein-protein interaction between large molecules.
- 社団法人 日本生化学会の論文
著者
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Park Sang-ho
College Of Pharmacy Seoul National University
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Kyogoku Yoshimasa
Institute For Protein Research Osaka University
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Lee Tae-woo
College Of Pharmacy Seoul National University
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Won Hyung-Sik
College of Pharmacr; Seoul National Unicersitl
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Lee Bong-Jin
College of Pharmacr; Seoul National Unicersitl
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