Kim E L, Maliuta S S
Institute of Molecular Biology and Genetics, Kiev, USSR.
FEBS Lett. 1989 Sep 25;255(2):361-4. doi: 10.1016/0014-5793(89)81122-6.
An S-adenosyl-L-methionine:DNA-methyltransferase, termed M.BnaI, was purified from Bacillus natto B3364 strain by successive column chromatography. The molecular weight determined by gel filtration was 37 kDa for M.BnaI. Analysis of methyltransferase by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed correspondence of the M.BnaI activity with one protein band at a molecular weight of 35 kDa. Sequencing of pUC19 DNA methylated with M.BnaI showed the cytosine-5 methylation in the BnaI recognition sequence GGAT decreases CC at the position indicated by the arrow.
一种名为M.BnaI的S-腺苷-L-甲硫氨酸：DNA甲基转移酶，通过连续柱色谱法从纳豆芽孢杆菌B3364菌株中纯化得到。通过凝胶过滤测定，M.BnaI的分子量为37 kDa。用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析甲基转移酶，结果显示M.BnaI活性与一条分子量为35 kDa的蛋白带相对应。用M.BnaI甲基化的pUC19 DNA测序表明，在BnaI识别序列GGAT中的胞嘧啶-5甲基化会使箭头所示位置的CC减少。
