The independent prokaryotic origins of eukaryotic fructose-1, 6-bisphosphatase and sedoheptulose-1, 7-bisphosphatase and the implications of their origins for the evolution of eukaryotic Calvin cycle.
The independent prokaryotic origins of eukaryotic fructose-1, 6-bisphosphatase and sedoheptulose-1, 7-bisphosphatase and the implications of their origins for the evolution of eukaryotic Calvin cycle.
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DOI：
10.1186/1471-2148-12-208
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发表时间：
2012-10-22
影响因子：
3.4
通讯作者：
Wen JF
中科院分区：
文献类型：
--
作者：
Jiang YH;Wang DY;Wen JF
在真细菌的卡尔文循环中，果糖-1，6-二磷酸（FBP）和景天庚酮糖-1，7-二磷酸（SBP）的脱磷酸化都是由同一个双功能酶催化的：果糖-1，6-二磷酸酶/景天庚酮糖-1，7-二磷酸酶（F/SBl），而在真核叶绿体中由两种不同的酶：叶绿体果糖-1，6-二磷酸酶（FBPase）和景天庚酮糖-1，7-二磷酸酶（SBPase）。有人提出，这两种真核生物酶产生的分歧，共同的祖先真细菌的线粒体起源的双功能F/SBYR。然而，在以前的系统发育分析中没有观察到SBB 1和真细菌FBPase或F/SBB 1之间的特异性亲和力，并且很难解释为什么SBB 1和/或F/SBB 1在大多数现存的非光合真核生物中不存在。结构域分析表明，两种不同来源的真细菌F/SBPases具有不同的结构域：蛋白细菌F/SBPases具有典型的FBPase结构域，而蓝藻F/SBPases具有FBPase_glpX结构域。因此，与原核生物FBPase一样，真细菌F/SBPase也可以分为两个进化上遥远的类别（I类和II类）。系统发育分析的基础上，一个更大的分类采样比以前的工作显示，所有真核生物SBP 3集群在一起，形成一个密切的姐妹组的进化枝的ε-蛋白细菌类FBPase的一类，这是一种细菌发生特异性的酶，而所有真核生物叶绿体FBPase组与真核细胞质FBPase一起，形成另一个不同的进化枝，然后与不同的真细菌类FBPase组。这些酶的基序分析也支持这些系统发育的相关性。有两个进化上遥远的类真细菌双功能F/SBB 1。真核生物的FBPase和SBPase没有从它们中的任何一个分离出来，而是有两个独立的起源：SBPase与ε-变形菌的细菌发生特异性I类FBPase共享一个共同的祖先（或者可能起源于ε-变形菌的祖先），而FBPase来自一种未知的真细菌的I类FBPase。在从真细菌I类FBPase进化而来的SBP 3的过程中，通过“从专家到通才”的转变获得了SBP 3-去磷酸化活性。这两种光调控底物特异性酶在进化上取代了内共生蓝藻的双功能F/SBB 1，使得卡尔文循环的调控更加精细，从而促进了真核光合作用乃至整个光合真核生物的进化。
In the Calvin cycle of eubacteria, the dephosphorylations of both fructose-1, 6-bisphosphate (FBP) and sedoheptulose-1, 7-bisphosphate (SBP) are catalyzed by the same bifunctional enzyme: fructose-1, 6-bisphosphatase/sedoheptulose-1, 7-bisphosphatase (F/SBPase), while in that of eukaryotic chloroplasts by two distinct enzymes: chloroplastic fructose-1, 6-bisphosphatase (FBPase) and sedoheptulose-1, 7-bisphosphatase (SBPase), respectively. It was proposed that these two eukaryotic enzymes arose from the divergence of a common ancestral eubacterial bifunctional F/SBPase of mitochondrial origin. However, no specific affinity between SBPase and eubacterial FBPase or F/SBPase can be observed in the previous phylogenetic analyses, and it is hard to explain why SBPase and/or F/SBPase are/is absent from most extant nonphotosynthetic eukaryotes according to this scenario. Domain analysis indicated that eubacterial F/SBPase of two different resources contain distinct domains: proteobacterial F/SBPases contain typical FBPase domain, while cyanobacterial F/SBPases possess FBPase_glpX domain. Therefore, like prokaryotic FBPase, eubacterial F/SBPase can also be divided into two evolutionarily distant classes (Class I and II). Phylogenetic analysis based on a much larger taxonomic sampling than previous work revealed that all eukaryotic SBPase cluster together and form a close sister group to the clade of epsilon-proteobacterial Class I FBPase which are gluconeogenesis-specific enzymes, while all eukaryotic chloroplast FBPase group together with eukaryotic cytosolic FBPase and form another distinct clade which then groups with the Class I FBPase of diverse eubacteria. Motif analysis of these enzymes also supports these phylogenetic correlations. There are two evolutionarily distant classes of eubacterial bifunctional F/SBPase. Eukaryotic FBPase and SBPase do not diverge from either of them but have two independent origins: SBPase share a common ancestor with the gluconeogenesis-specific Class I FBPase of epsilon-proteobacteria (or probably originated from that of the ancestor of epsilon-proteobacteria), while FBPase arise from Class I FBPase of an unknown kind of eubacteria. During the evolution of SBPase from eubacterial Class I FBPase, the SBP-dephosphorylation activity was acquired through the transition “from specialist to generalist”. The evolutionary substitution of the endosymbiotic-origin cyanobacterial bifunctional F/SBPase by the two light-regulated substrate-specific enzymes made the regulation of the Calvin cycle more delicate, which contributed to the evolution of eukaryotic photosynthesis and even the entire photosynthetic eukaryotes.
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