| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2010: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2009: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Research Abstract |
The present study assessed the contribution of sctive site sequence of Escherichia coli DsbA by screening a library of mutant dsbA genes with the genetically randomized active-site sequence CXXC. Alleles of 24 dsbA mutants gave significant variation in the cellular functions, and a mutant dsbA gene that encodes Cys-Asp-Ile-Cys sequence enhanced pahge sensitivity by 40-fold more than the wild-type dsbA. The redox potential of DsbA[CDIC] was determined to be. 171. 8 mV, which suggested less oxidizing catalyst than the wild type DsbA(-125. 9 mV) and the redox potential was close to that of yeast protein disulfide isomerase(175 mV). It was suggested that DsbA[CDIC] improved the net yield of the correctly folded periplasmic proteins through the disulfide isomerase catalysis. Thermostable homologs were also characterized for application of folding catalysis at high temperature.
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