Molecular Evolution of the Oxygen-Binding Hemerythrin Domain.
Molecular Evolution of the Oxygen-Binding Hemerythrin Domain.
复制标题
DOI：
10.1371/journal.pone.0157904
复制
发表时间：
2016
期刊：
影响因子：
3.7
通讯作者：
Lazcano A
中科院分区：
文献类型：
--
作者：
Alvarez-Carreño C;Becerra A;Lazcano A
在前寒武纪时期，充氧光合作用的演变需要采取多样化的策略，最大限度地减少与活性氧物种相关的损害。已知四个氧载体蛋白家族(血红蛋白、杂氰菊酯以及节肢动物和软体动物血蓝蛋白两个非同源家族)已独立进化出与氧可逆结合的能力，为细胞提供了应对氧气积累的进化压力的策略。氧结合杂氰菊酯最初是在海洋无脊椎动物中研究的，但进一步的研究表明，它存在于生命的三个领域，这有力地表明，它的起源早于真核生物的出现。氧结合杂草菊酯是组氨酸、组氨酸、谷氨酸阳离子结合域的一个单系亚基。氧结合杂氰菊酯同系物在367/2236细菌、21/150古生菌和4/135真核基因组中被明确鉴定。总体而言，氧结合杂氰菊酯同系物被发现与单结构域和长蛋白质序列的比例相同。在长菊酯序列中，蛋白质结构域的相关功能可分为三大类：信号转导、磷传递反应调节和蛋白质结合。这表明在许多生物体中，可逆的氧结合能力被合并到信号通路中。氧结合杂氰菊酯同系物的最大似然树揭示了一个复杂的进化史，其中侧向基因转移、复制和基因丢失似乎发挥了重要作用。杂氰菊酯是一个古老的蛋白质结构域，有着复杂的进化史。在原核生物中，结合氧的杂氰菊酯的独特的铁结合配位位点最早进化，很可能是在Firmicuts和变形杆菌分化之前，并传播到许多细菌、古生物和真核生物中。在原核生物和真核生物中，氧结合结构域的后期进化导致了广泛的功能，从在厌氧和微好氧生物中保护免受氧化损伤，到在有氧和兼性物种中向特定的酶和途径供氧。
The evolution of oxygenic photosynthesis during Precambrian times entailed the diversification of strategies minimizing reactive oxygen species-associated damage. Four families of oxygen-carrier proteins (hemoglobin, hemerythrin and the two non-homologous families of arthropodan and molluscan hemocyanins) are known to have evolved independently the capacity to bind oxygen reversibly, providing cells with strategies to cope with the evolutionary pressure of oxygen accumulation. Oxygen-binding hemerythrin was first studied in marine invertebrates but further research has made it clear that it is present in the three domains of life, strongly suggesting that its origin predated the emergence of eukaryotes. Oxygen-binding hemerythrins are a monophyletic sub-group of the hemerythrin/HHE (histidine, histidine, glutamic acid) cation-binding domain. Oxygen-binding hemerythrin homologs were unambiguously identified in 367/2236 bacterial, 21/150 archaeal and 4/135 eukaryotic genomes. Overall, oxygen-binding hemerythrin homologues were found in the same proportion as single-domain and as long protein sequences. The associated functions of protein domains in long hemerythrin sequences can be classified in three major groups: signal transduction, phosphorelay response regulation, and protein binding. This suggests that in many organisms the reversible oxygen-binding capacity was incorporated in signaling pathways. A maximum-likelihood tree of oxygen-binding hemerythrin homologues revealed a complex evolutionary history in which lateral gene transfer, duplications and gene losses appear to have played an important role. Hemerythrin is an ancient protein domain with a complex evolutionary history. The distinctive iron-binding coordination site of oxygen-binding hemerythrins evolved first in prokaryotes, very likely prior to the divergence of Firmicutes and Proteobacteria, and spread into many bacterial, archaeal and eukaryotic species. The later evolution of the oxygen-binding hemerythrin domain in both prokaryotes and eukaryotes led to a wide variety of functions, ranging from protection against oxidative damage in anaerobic and microaerophilic organisms, to oxygen supplying to particular enzymes and pathways in aerobic and facultative species.