| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10235299 | Process Biochemistry | 2014 | 16 Pages |
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.
- 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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
S.V. Tarlachkov, O.V. Dyachenko, A.M. Cherevatenko, N.V. Rudenko, T.V. Shevchuk,