Bujnicki J M
Henry Ford Health System, Molecular Biology Research Program, Detroit, MI 48202, USA.
Acta Microbiol Pol. 2000;49(1):19-29.
The Escherichia coli PrmA enzyme catalyzes methylation of the large ribosomal subunit protein L11. Database homology searches, multiple sequence alignment, and structure prediction allowed to dissect the primary structure of PrmA into two domains and assign putative functional or structural roles to invariant or highly conserved residues. Evolutionary relationships within the PrmA family were also analyzed. The topology of the branching order agrees to a large extent with the consensus phylogeny of Eubacteria, with the exception of beta and epsilon subdivisions of Proteobacteria, which most probably had their original prmA genes replaced by copies acquired via the lateral gene transfer from gamma-Proteobacteria and some close relative of the ancestor of gramnegative bacteria, respectively.
大肠杆菌的PrmA酶催化大核糖体亚基蛋白L11的甲基化。通过数据库同源性搜索、多序列比对和结构预测，可将PrmA的一级结构剖析为两个结构域，并为不变或高度保守的残基赋予假定的功能或结构作用。还分析了PrmA家族内的进化关系。分支顺序的拓扑结构在很大程度上与真细菌的共识系统发育一致，但变形菌门的β和ε亚群除外，它们很可能分别通过从γ-变形菌和革兰氏阴性菌祖先的一些近亲通过横向基因转移获得的拷贝取代了其原始的prmA基因。
