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M.EaeI 甲基化修饰酶的分离与鉴定

Isolation and characterization of the M.EaeI modification methylase.

作者信息

Jacobs D, Brown N L

出版信息

Biochem J. 1986 Sep 1;238(2):613-5. doi: 10.1042/bj2380613.

Abstract

The modification enzyme (M.EaeI) corresponding to the restriction endonuclease EaeI was partially purified from Enterobacter aerogenes PW201. The M.EaeI enzyme methylates the innermost cytosine residue in each strand of the family of related sequences that constitute the EaeI recognition site to give: 5'-Y-G-G-5mC-C-R-3' where 5mC is 5-methylcytosine. M.EaeI protects these sites against cleavage by HaeIII, and protects overlapping 5'-C-C-G-G-3' sites against cleavage by both HpaII and MspI.

摘要

与限制性内切酶EaeI相对应的甲基化酶(M.EaeI)从产气肠杆菌PW201中部分纯化得到。M.EaeI酶将构成EaeI识别位点的相关序列家族每条链中最内侧的胞嘧啶残基甲基化,生成:5'-Y-G-G-5mC-C-R-3',其中5mC为5-甲基胞嘧啶。M.EaeI保护这些位点不被HaeIII切割,并保护重叠位点5'-C-C-G-G-3'不被HpaII和MspI切割。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/da07/1147176/c019d649b47e/biochemj00272-0293-a.jpg

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