Affinity Selection of DNA-Binding Proteins Displayed on Bacteriophage .LAMBDA..
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概要
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Two transcription factors, human ATF 1, its DNA-binding domain (ATFIBD), and the DNA-binding domain (GAL 4 BD) of the yeast GAL 4 protein, were displayed on the surface of bacteriophage λ vectors and efficiently selected by DNA fragments immobilized in microtiter wells. The DNA-binding proteins are fused to the carboxy terminus of the tail protein gpV and head protein gpD of the vectors, λfoo and λfooDc, respectively. After a single round of affinity selection, the fusion phages were successfully enriched 60- to 4, 000-fold over the vector phages. Further, the GAL 4 BD fusion phages were enriched 5- and 15-fold by affinity selection using specific DNA as probes over nonspecific DNA when expressed on AfooDc and λfoo, respectively. The ATF 1 BD fusion phages were also sequence-specifically enriched greater than 4-fold when displayed on λfoo. These results suggest that the λfoo display system is useful for in vitro studying of protein-DNA interactions and may be applied to screening of DNA-binding protein from complex cDNA libraries through DNA-binding affinity.
- 社団法人 日本生化学会の論文
著者
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ZHANG Yan
Department Molecular Oral Medicine and Maxillofacial Surgery, Division of Frontier Medical Science,
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PAK Jeong
Department of Molecular Biology, National Institute of Bioscience and Human Technology
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MACHIDA Masayuki
Department of Agricultural Chemistry, The University of Tokyo
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Maruyama Ichiro
Department of Pharmacology, Hokuriku University, School of Pharmacy
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- Affinity Selection of DNA-Binding Proteins Displayed on Bacteriophage .LAMBDA..