Bujnicki J M, Radlinska M
Molecular Biology Research Program, Henry Ford Health System, Detroit, Michigan 48202, USA.
IUBMB Life. 1999 Sep;48(3):247-9. doi: 10.1080/713803519.
Previous comparative studies revealed close similarity among various groups of S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases (MTases), indicating their common evolutionary origin. We present evidence for a remarkable similarity between the sequence and predicted structure of HemK (a widespread family of putative proteins encoded in genomes from bacteria to humans) and the catalytic domain of the gamma-subfamily of adenine-specific DNA MTases (N6mA MTases). We predict the structure and function of the putative catalytic domain of HemK proteins and speculate that the target-recognizing function may be conferred by the N-terminal variable region.
以往的比较研究表明，各种依赖S-腺苷-L-甲硫氨酸（AdoMet）的甲基转移酶（MTases）之间存在密切的相似性，这表明它们有着共同的进化起源。我们提供了证据，证明HemK（从细菌到人类基因组中广泛编码的一类推定蛋白质）的序列和预测结构与腺嘌呤特异性DNA甲基转移酶（N6mA MTases）γ亚家族的催化结构域之间存在显著相似性。我们预测了HemK蛋白推定催化结构域的结构和功能，并推测靶标识别功能可能由N端可变区赋予。
