Abstract
Design of the transcriptionally-fused protein M•HhaI-EGFP, composed of bacterial DNA-methyltransferase M•HhaI and enhanced green fluorescent protein (GFP) is described. The mentioned M•HhaI-EGFP was expressed in Escherichia coli ER1821 and purified by affinity chromatography on Ni-NTA agarose. According to expectations M•HhaI-EGFP fused protein retained significant features of corresponding original proteins: the ability to transfer methyl group to the C5 carbon atom of internal cytosine in CGCG site and absorption–emission spectral characteristics. The created transcriptionally-fused protein M•HhaI-EGFP could be used in various experiments in molecular biology.
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