Evolution of two-component signal transduction

Evolution of two-component signal transduction
复制标题

DOI:
10.1093/oxfordjournals.molbev.a026297
复制
发表时间:
2000-12-01
影响因子:
10.7
通讯作者:
Brown, JR
Brown, JR
中科院分区:
生物学1区
文献类型:
--
作者:
Koretke, KK;Lupas, AN;Brown, JR

文献摘要

被引文献

相似文献

双组分信号转导(TCST)系统是协调细菌以及一些植物、真菌、原生动物和古生菌对环境变化反应的主要手段。这些系统通常由受体组氨酸激酶组成,它通过磷酸化细胞质反应调节器对细胞外信号做出反应,导致细胞行为的改变。虽然包括产孢子和趋化作用在内的几个模型系统已经被广泛研究,但特定的TCST系统之间的进化关系还不是很清楚,信号转导组件的起源也不清楚。用距离法构建了14个完整基因组和6个部分基因组的TCST组分的系统发育树,包括183个组氨酸激酶和220个反应调节子。这些树在11个可识别的系统发育簇的位置上显示出广泛的一致性。真核序列几乎只存在于一个簇中,在其组成蛋白中也显示出最大程度的结构域变异,而古生菌序列主要形成物种特有的簇。激酶树不同部分的三个簇包含具有丝氨酸磷酸化活性的蛋白质。所有的激酶都被发现相对于它们的超家族的其他成员是单系的,例如Il拓扑异构酶和Hsp90。结构分析进一步表明,它与真核蛋白激酶的ATP结合区有很大的相似性。TCST系统来源于细菌,通过横向基因转移辐射到古生菌和真核生物中。它们的成分显示出广泛的共同进化,表明重组并不是它们分化的主要因素。尽管组氨酸激酶活性普遍存在,但丝氨酸激酶在这个家族中已经独立进化了多次,并伴随着同源反应调节因子的丧失(S)。TCST激酶和真核蛋白激酶在结构和功能上的相似性增加了它们之间进化关系的可能性。
Two-component signal transduction (TCST) systems are the principal means for coordinating responses to environmental changes in bacteria as well as some plants, fungi, protozoa, and archaea. These systems typically consist of a receptor histidine kinase, which reacts to an extracellular signal by phosphorylating a cytoplasmic response regulator, causing a change in cellular behavior. Although several model systems, including sporulation and chemotaxis, have been extensively studied, the evolutionary relationships between specific TCST systems are not well understood, and the ancestry of the signal transduction components is unclear. Phylogenetic trees of TCST components from 14 complete and 6 partial genomes, containing 183 histidine kinases and 220 response regulators, were constructed using distance methods. The trees showed extensive congruence in the positions of 11 recognizable phylogenetic clusters. Eukaryotic sequences were found almost exclusively in one cluster, which also showed the greatest extent of domain variability in its component proteins, and archaeal sequences mainly formed species-specific clusters. Three clusters in different parts of the kinase tree contained proteins with serine-phosphorylating activity. All kinases were found to be monophyletic with respect to other members of their superfamily, such as type Il topoisomerases and Hsp90. Structural analysis further revealed significant similarity to the ATP-binding domain of eukaryotic protein kinases. TCST systems are of bacterial origin and radiated into archaea and eukaryotes by lateral gene transfer. Their components show extensive coevolution, suggesting that recombination has not been a major factor in their differentiation. Although histidine kinase activity is prevalent, serine kinases have evolved multiple times independently within this family, accompanied by a loss of the cognate response regulator(s). The structural and functional similarity between TCST kinases and eukaryotic protein kinases raises the possibility of a distant evolutionary relationship.