Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms
Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms
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DOI：
10.1007/pl00006177
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发表时间：
1997-05-01
影响因子：
3.9
通讯作者：
Karlin, S
中科院分区：
文献类型：
--
作者：
Brendel, V;Brocchieri, L;Karlin, S
与大肠杆菌 RecA 相似的蛋白质序列在真细菌、古细菌和真核生物的主要界中进行了比较。古细菌序列单系分支，与真核旁系同源 Rad51 和 Dmc1 群关系最密切。序列的多重比对表明 RecA 样蛋白的模块化结构由不同的片段组成，其中一些片段仅在序列亚组内保守。真核生物和古细菌序列共享一个 N 末端结构域，该结构域可能在与其他因子和核酸的相互作用中发挥作用。比对块中的几个位置在作为一组的真细菌内以及作为第二组的真核生物和古细菌内高度保守，但在各组之间进行比较时，这些位置显示出非保守氨基酸取代。 RecA 样核心结构域内的保守性鉴定了参与 ATP 诱导的构象变化的可能关键残基。我们提出，RecA 样蛋白在进化上源自各种独立结构域，并且非真细菌中 RecA 的功能同源物包含一系列串联或协同作用的 RecA 样蛋白。
Protein sequences with similarities to Escherichia coli RecA were compared across the major kingdoms of eubacteria, archaebacteria, and eukaryotes. The archaeal sequences branch monophyletically and are most closely related to the eukaryotic paralogous Rad51 and Dmc1 groups. A multiple alignment of the sequences suggests a modular structure of RecA-like proteins consisting of distinct segments, some of which are conserved only within subgroups of sequences. The eukaryotic and archaeal sequences share an N-terminal domain which may play a role in interactions with other factors and nucleic acids. Several positions in the alignment blocks are highly conserved within the eubacteria as one group and within the eukaryotes and archaebacteria as a second group, but compared between the groups these positions display nonconservative amino acid substitutions. Conservation within the RecA-like core domain identifies possible key residues involved in ATP-induced conformational changes. We propose that RecA-like proteins derive evolutionarily from an assortment of independent domains and that the functional homologs of RecA in noneubacteria comprise an array of RecA-like proteins acting in series or cooperatively.