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• W2083175091 endingPage "196" @default.
• W2083175091 startingPage "189" @default.
• W2083175091 abstract "An efficient Escherichia coli expression system was constructed for the production of a variant form of HNF1 protein having the additional five amino acid residues (Asp-Arg-Trp-Gly-Ser) at the NH(2)-terminal. The cDNA encoding HNF1 was ligated to 6 x His tag and inserted into an inducible bacterial expression vector pRSET A. After expression in E. coli, the recombinant product was purified by Ni-NTA affinity column chromatography. The purified product showed expected NH(2)-terminal sequence and specific binding to the HNF1 site. The effect of pyridoxal 5'-phosphate and its analogues on the binding activity of recombinant HNF1 was examined and found that only pyridoxal 5'-phosphate effectively inhibited the DNA binding. The concentration of pyridoxal 5'-phosphate that inhibited 50% of DNA binding was around 100 microM. Furthermore, we identified Lys197 of HNF1 molecule as the essential residue of DNA binding. These observations suggest that pyridoxal 5'-phosphate directly interacts with tissue-specific transcription factor HNF1 and modulates the binding to DNA." @default.
• W2083175091 created "2016-06-24" @default.
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• W2083175091 date "2001-12-01" @default.
• W2083175091 modified "2023-09-26" @default.
• W2083175091 title "Pyridoxal 5′-phosphate inhibits DNA binding of HNF1" @default.
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• W2083175091 doi "https://doi.org/10.1016/s0304-4165(01)00221-5" @default.
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