IHB OpenIR  > 期刊论文
Origin and evolution of the RIG-I like RNA helicase gene family
Zou, Jun; Chang, Mingxian; Nie, Pin; Secombes, Chris J.; Zou, J, Univ Aberdeen, Sch Biol Sci, Scottish Fish Immunol Res Ctr, Aberdeen AB24 2TZ, Scotland
2009
Source PublicationBMC EVOLUTIONARY BIOLOGY
Volume9
AbstractBackground: The DExD/H domain containing RNA helicases such as retinoic acid-inducible gene I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5) are key cytosolic pattern recognition receptors (PRRs) for detecting nucleotide pathogen associated molecular patterns (PAMPs) of invading viruses. The RIG-I and MDA5 proteins differentially recognise conserved PAMPs in double stranded or single stranded viral RNA molecules, leading to activation of the interferon system in vertebrates. They share three core protein domains including a RNA helicase domain near the C terminus (HELICc), one or more caspase activation and recruitment domains (CARDs) and an ATP dependent DExD/H domain. The RIG-I/MDA5 directed interferon response is negatively regulated by laboratory of genetics and physiology 2 (LGP2) and is believed to be controlled by the mitochondria antiviral signalling protein (MAVS), a CARD containing protein associated with mitochondria. Results: The DExD/H containing RNA helicases including RIG-I, MDA5 and LGP2 were analysed in silico in a wide spectrum of invertebrate and vertebrate genomes. The gene synteny of MDA5 and LGP2 is well conserved among vertebrates whilst conservation of the gene synteny of RIG-I is less apparent. Invertebrate homologues had a closer phylogenetic relationship with the vertebrate RIG-Is than the MDA5/LGP2 molecules, suggesting the RIG-I homologues may have emerged earlier in evolution, possibly prior to the appearance of vertebrates. Our data suggest that the RIG-I like helicases possibly originated from three distinct genes coding for the core domains including the HELICc, CARD and ATP dependent DExD/H domains through gene fusion and gene/domain duplication. Furthermore, presence of domains similar to a prokaryotic DNA restriction enzyme III domain (Res III), and a zinc finger domain of transcription factor (TF) IIS have been detected by bioinformatic analysis. Conclusion: The RIG-I/MDA5 viral surveillance system is conserved in vertebrates. The RIG-I like helicase family appears to have evolved from a common ancestor that originated from genes encoding different core functional domains. Diversification of core functional domains might be fundamental to their functional divergence in terms of recognition of different viral PAMPs.
KeywordDouble-stranded-rna Antiviral Responses Innate Immunity Recognition Domain Lgp2 Elongation Receptors Mechanism Cleavage
Department[Zou, Jun; Chang, Mingxian; Secombes, Chris J.] Univ Aberdeen, Sch Biol Sci, Scottish Fish Immunol Res Ctr, Aberdeen AB24 2TZ, Scotland; [Chang, Mingxian; Nie, Pin] Chinese Acad Sci, State Key Lab Freshwater Ecol, Wuhan 430072, Peoples R China; [Chang, Mingxian; Nie, Pin] Chinese Acad Sci, Biotechnol Inst Hydrobiol, Wuhan 430072, Peoples R China
Subject AreaEvolutionary Biology ; Genetics & Heredity
Funding OrganizationRoyal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083]
Indexed Bysci
Language英语
WOS IDBMC:10.1186/1471-2148-9-85
Funding OrganizationRoyal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083] ; Royal Society of Edinburgh and National Natural Science Foundation of China [30711130225, 30830083]
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/152342/7720
Collection期刊论文
Corresponding AuthorZou, J, Univ Aberdeen, Sch Biol Sci, Scottish Fish Immunol Res Ctr, Aberdeen AB24 2TZ, Scotland
Recommended Citation
GB/T 7714
Zou, Jun,Chang, Mingxian,Nie, Pin,et al. Origin and evolution of the RIG-I like RNA helicase gene family[J]. BMC EVOLUTIONARY BIOLOGY,2009,9.
APA Zou, Jun,Chang, Mingxian,Nie, Pin,Secombes, Chris J.,&Zou, J, Univ Aberdeen, Sch Biol Sci, Scottish Fish Immunol Res Ctr, Aberdeen AB24 2TZ, Scotland.(2009).Origin and evolution of the RIG-I like RNA helicase gene family.BMC EVOLUTIONARY BIOLOGY,9.
MLA Zou, Jun,et al."Origin and evolution of the RIG-I like RNA helicase gene family".BMC EVOLUTIONARY BIOLOGY 9(2009).
Files in This Item:
File Name/Size DocType Version Access License
Origin and evolution(440KB) 开放获取--View Application Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Zou, Jun]'s Articles
[Chang, Mingxian]'s Articles
[Nie, Pin]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zou, Jun]'s Articles
[Chang, Mingxian]'s Articles
[Nie, Pin]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zou, Jun]'s Articles
[Chang, Mingxian]'s Articles
[Nie, Pin]'s Articles
Terms of Use
No data!
Social Bookmark/Share
File name: Origin and evolution of the RIG-I like RNA helicase gene family.pdf
Format: Adobe PDF
This file does not support browsing at this time
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.