Karreman C, de Waard A
Sylvius Laboratories, Department of Medical Biochemistry, University of Leiden, The Netherlands.
J Bacteriol. 1990 Jan;172(1):266-72. doi: 10.1128/jb.172.1.266-272.1990.
The complete type II modification methylase of Agmenellum quadruplicatum was cloned in Escherichia coli as an R.Sau3A fragment of approximately 4.5 kilobases. The coding sequence was contained in a stretch of 1,156 base pairs which was organized into two parallel, partly overlapping open reading frames of 248 and 139 codons. In vivo complementation experiments showed that the synthesis of both predicted peptides was required for full methylase activity. The amino acid sequences were considerably similar to regions of other deoxycytidylate methylases.
嗜热栖热放线菌完整的II型修饰甲基化酶作为一个约4.5千碱基的Sau3A片段在大肠杆菌中被克隆。编码序列包含在一段1156个碱基对中，该序列被组织成两个平行的、部分重叠的开放阅读框，分别为248和139个密码子。体内互补实验表明，两种预测肽的合成对于完整的甲基化酶活性是必需的。氨基酸序列与其他脱氧胞苷酸甲基化酶的区域有相当大的相似性。
