淋病奈瑟菌MS11中两个串联排列的DNA甲基转移酶基因的结构表征：N4-胞嘧啶特异性M.NgoMXV和无功能的5-胞嘧啶型M.NgoMorf2P。

Structural characterization of two tandemly arranged DNA methyltransferase genes from Neisseria gonorrhoeae MS11: N4-cytosine specific M.NgoMXV and nonfunctional 5-cytosine-type M.NgoMorf2P.

作者信息

Radlinska M, Bujnicki J M, Piekarowicz A

机构信息

Institute of Microbiology, University of Warsaw, Poland.

出版信息

Proteins. 1999 Dec 1;37(4):717-28. doi: 10.1002/(sici)1097-0134(19991201)37:4<717::aid-prot20>3.0.co;2-p.

DOI:10.1002/(sici)1097-0134(19991201)37:4<717::aid-prot20>3.0.co;2-p

PMID:10651285

Abstract

Two adjacent genes encoding DNA methyltransferases (MTases) of Neisseria gonorrhoeae MS11, an active N4-cytosine specific M. NgoMXV and an inactive 5-cytosine type M. NgoMorf2P, were cloned into Escherichia coli and sequenced. We analyzed the deduced amino acid sequence of both gene products and localized conserved regions characteristic for DNA MTases. Structure prediction, threading-derived alignments, and comparison with the common fold for DNA MTases allowed for construction of super-secondary and tertiary models for M.NgoMorf2P and M.NgoMXV, respectively. These models helped in identification of amino acids and structural elements essential for function of both enzymes. The implications of this putative structural model on the catalytic mechanism of M.NgoMXV and its possible relation to the common ancestor of modern DNA amino-MTases are also discussed.

摘要

淋病奈瑟菌MS11中两个相邻的编码DNA甲基转移酶（MTases）的基因被克隆到大肠杆菌中并进行测序，这两个基因分别是具有活性的N4-胞嘧啶特异性的NgoMXV和无活性的5-胞嘧啶类型的NgoMorf2P。我们分析了这两个基因产物推导的氨基酸序列，并定位了DNA MTases特有的保守区域。通过结构预测、穿线比对以及与DNA MTases的常见折叠结构进行比较，分别构建了NgoMorf2P和NgoMXV的超二级和三级模型。这些模型有助于鉴定这两种酶功能所必需的氨基酸和结构元件。本文还讨论了这种假定的结构模型对NgoMXV催化机制的影响及其与现代DNA氨基-MTases共同祖先的可能关系。