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제안 방법
- Houston- 1, CAF27185; Ectocarpus siliculosus virus EsV-1-64, AAK14487; Feldmannia irregularis virus FirrV-l-B43, AAR26918; Acanthamoeba polyphaga mimivirus, AAV50623; 8 coli APEC, 01ABJ00523; Bacteriophage VT2-Sa, BAA84296; and Phage BP-4795, CAD88815. A sequence similarity search was performed 냐sing the BLAST program of the National Center for Biotechnology Information (NCBI), and multiple protein sequence alignment was conducted using the CLUS1ALW program (http://www. ebi.ac.uk/clustalw).
- BioRad, USA). All experiments were repeated three times, and the mean values were used for data analysis.
- However, no functional experiments regarding this protein have been performed. In this paper, we amplified this putative exonuclease gene through PCR, cloned and expressed it in Escherichia coll as a recombinant protein, and tested its activities using various DNA substrates.
- In this study, we expressed a chorella virus SS-2 nuclease in E. coil and tested its activity using various DNA substrates. It is known tliat each individual nuclease displays a preference for specific substrates and sites.
- To find the optimal conditions for SS-2 nuclease, temperatures, pH concentration, and different divalent ions were tested. SS-2 nuclease displayed stable activity at a wide range of temperatures, between 10-50℃ (Fig.
- Most expressed protein was found in the insoluble cell pellet. To increase the solubility of the recombinant protein, changes of culture conditions, bacterial host strain, concentrations of IPTQ incubation temperatures, and induction times were used (data not shown). Although the majority of the SS-2 nuclease was still produced in an insoluble form, coexpression of SS-2 nuclease with molecular chaperone protein, using the chaperone-containing expression host pKJE7 cells, appeared to enhance the soluble expression.
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