Genome-wide analysis of putative peroxiredoxin in unicellular and filamentous cyanobacteria | |
Cui, Hongli1,2; Wang, Yipeng1; Wang, Yinchu1,2; Qin, Song1 | |
发表期刊 | BMC EVOLUTIONARY BIOLOGY |
ISSN | 1471-2148 |
2012-11-16 | |
卷号 | 12页码:220 |
关键词 | Peroxiredoxin Structure Phylogeny And Evolution Comparative Genomics Cyanobacteria |
产权排序 | [Cui, Hongli; Wang, Yipeng; Wang, Yinchu; Qin, Song] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China; [Cui, Hongli; Wang, Yinchu] Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
通讯作者 | Qin, S (reprint author), Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China. |
作者部门 | 海岸带生物学与生物资源利用所重点实验室 |
英文摘要 | Background: Cyanobacteria are photoautotrophic prokaryotes with wide variations in genome sizes and ecological habitats. Peroxiredoxin (PRX) is an important protein that plays essential roles in protecting own cells against reactive oxygen species (ROS). PRXs have been identified from mammals, fungi and higher plants. However, knowledge on cyanobacterial PRXs still remains obscure. With the availability of 37 sequenced cyanobacterial genomes, we performed a comprehensive comparative analysis of PRXs and explored their diversity, distribution, domain structure and evolution. Results: Overall 244 putative prx genes were identified, which were abundant in filamentous diazotrophic cyanobacteria, Acaryochloris marina MBIC 11017, and unicellular cyanobacteria inhabiting freshwater and hot-springs, while poor in all Prochlorococcus and marine Synechococcus strains. Among these putative genes, 25 open reading frames (ORFs) encoding hypothetical proteins were identified as prx gene family members and the others were already annotated as prx genes. All 244 putative PRXs were classified into five major subfamilies (1-Cys, 2-Cys, BCP, PRX5_like, and PRX-like) according to their domain structures. The catalytic motifs of the cyanobacterial PRXs were similar to those of eukaryotic PRXs and highly conserved in all but the PRX-like subfamily. Classical motif (CXXC) of thioredoxin was detected in protein sequences from the PRX-like subfamily. Phylogenetic tree constructed of catalytic domains coincided well with the domain structures of PRXs and the phylogenies based on 16s rRNA. Conclusions: The distribution of genes encoding PRXs in different unicellular and filamentous cyanobacteria especially those sub-families like PRX-like or 1-Cys PRX correlate with the genome size, eco-physiology, and physiological properties of the organisms. Cyanobacterial and eukaryotic PRXs share similar conserved motifs, indicating that cyanobacteria adopt similar catalytic mechanisms as eukaryotes. All cyanobacterial PRX proteins share highly similar structures, implying that these genes may originate from a common ancestor. In this study, a general framework of the sequence-structure-function connections of the PRXs was revealed, which may facilitate functional investigations of PRXs in various organisms.; Background: Cyanobacteria are photoautotrophic prokaryotes with wide variations in genome sizes and ecological habitats. Peroxiredoxin (PRX) is an important protein that plays essential roles in protecting own cells against reactive oxygen species (ROS). PRXs have been identified from mammals, fungi and higher plants. However, knowledge on cyanobacterial PRXs still remains obscure. With the availability of 37 sequenced cyanobacterial genomes, we performed a comprehensive comparative analysis of PRXs and explored their diversity, distribution, domain structure and evolution. |
文章类型 | Article |
资助机构 | National Natural Science Foundation of China [40876082]; International Innovation Partnership Program: Typical Environmental Process and Effects on Resources in Coastal Zone Area; Public Science and Technology Research Funds Projects of the Ocean [200905021-3]; Outstanding Young Scholars Fellowship of Shandong Province [JQ200914] |
收录类别 | SCI |
语种 | 英语 |
关键词[WOS] | ALKYL HYDROPEROXIDE REDUCTASE ; SYNECHOCYSTIS SP PCC-6803 ; ESCHERICHIA-COLI ; CATALASE-PEROXIDASE ; CRYSTAL-STRUCTURE ; OXIDATIVE STRESS ; TRYPAREDOXIN PEROXIDASE ; MAMMALIAN PEROXIREDOXIN ; OXYGENIC PHOTOSYNTHESIS ; PLANT PEROXIREDOXINS |
研究领域[WOS] | Evolutionary Biology ; Genetics & Heredity |
WOS记录号 | WOS:000312135900001 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.yic.ac.cn/handle/133337/6108 |
专题 | 海岸带生物学与生物资源利用重点实验室_海岸带生物学与生物资源保护实验室 |
作者单位 | 1.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
推荐引用方式 GB/T 7714 | Cui, Hongli,Wang, Yipeng,Wang, Yinchu,et al. Genome-wide analysis of putative peroxiredoxin in unicellular and filamentous cyanobacteria[J]. BMC EVOLUTIONARY BIOLOGY,2012,12:220. |
APA | Cui, Hongli,Wang, Yipeng,Wang, Yinchu,&Qin, Song.(2012).Genome-wide analysis of putative peroxiredoxin in unicellular and filamentous cyanobacteria.BMC EVOLUTIONARY BIOLOGY,12,220. |
MLA | Cui, Hongli,et al."Genome-wide analysis of putative peroxiredoxin in unicellular and filamentous cyanobacteria".BMC EVOLUTIONARY BIOLOGY 12(2012):220. |
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