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Phylogenetic analysis of Na+/K+ ATPase: Insight into the mechanism for the genesis of multi-isoforms of protein complex
Ma, F; Huang, HF; Lin, LP; Xue, CH; Li-Ling, J; Chen, LM; Wang, YQ; Li, QW; Li, YD
Source PublicationJOURNAL OF BIOLOGICAL SYSTEMS
2005-09-01
Volume13Issue:3Pages:299-312
SubtypeArticle
AbstractOne most notable trend during the evolution is the substantial expansion of genomes along with dramatic expansion of protein diversity. It has been discovered that, whilst in prokaryotes subunits of many proteinases axe encoded by single genes, these are mostly encoded by multi-genes in eukaryotes. To understand the mechanism for the genesis of multi-isoforms of protein complex, we have analyzed amino acid sequences of Na+/K+ ATPase from various species ranging from archaea to vertebrates. Phylogenetic relationship between the selected species was considered from the perspective of important functional domains of Na+/K+ ATPase including cation ATPase N termination, E1-E2 ATPase, hydrolase, and cation ATPase C termination of the a subunit, Na+/K+ ATPase of the beta subunit, and ATP1G1_PLM_MAT8 of the gamma subunit. Coincident trees, obtained through comparison of aforementioned domains of the alpha and beta subunits, were used to examine the evolutionary divergence. By conservational and phylogenetic analyses, evolution of the Na+/K+ ATPase was outlined. Evidence was also found that essential domains of the Na+/K+ ATPase have been conserved during the evolution. These investigations seem to imply that various isoforms of alpha and beta subunits of vertebral Na+/K+ ATPases have evolved from single ancestral alpha and beta subunit genes through duplication events. In addition, our results seem to suggest a third fate for duplicated genes, e.g. the duplicate may have the same function as their ancestor gene. The results may also provide important clues to the underlying mechanisms of genesis of Na+/K+ ATPase multi-isoforms.
Keywordna+/k+ Atpase Phylogenetic Analysis Functional Domain Evolution Gene Duplication
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS KeywordP-TYPE ATPASES ; EVOLUTION ; ORGANIZATION ; NA,K-ATPASE
Indexed BySCI
Language英语
WOS Research AreaLife Sciences & Biomedicine - Other Topics ; Mathematical & Computational Biology
WOS SubjectBiology ; Mathematical & Computational Biology
WOS IDWOS:000232283500006
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ia.ac.cn/handle/173211/9169
Collection09年以前成果
Affiliation1.Liaoning Normal Univ, Coll Life Sci, Lab Comparat Genome & Bioinformat, Dalian 116029, Peoples R China
2.Xiamen Univ, Sch Life Sci, Xiamen 361005, Peoples R China
3.Tsinghua Univ, Dept Automat, MOE Key Lab Bioinformat, Beijing 100084, Peoples R China
4.Chinese Acad Sci, Inst Automat, Lab Complex Syst & Intelligence Sci, Beijing 100080, Peoples R China
5.China Med Univ, Dept Med Genet, Shenyang 110001, Peoples R China
Recommended Citation
GB/T 7714
Ma, F,Huang, HF,Lin, LP,et al. Phylogenetic analysis of Na+/K+ ATPase: Insight into the mechanism for the genesis of multi-isoforms of protein complex[J]. JOURNAL OF BIOLOGICAL SYSTEMS,2005,13(3):299-312.
APA Ma, F.,Huang, HF.,Lin, LP.,Xue, CH.,Li-Ling, J.,...&Li, YD.(2005).Phylogenetic analysis of Na+/K+ ATPase: Insight into the mechanism for the genesis of multi-isoforms of protein complex.JOURNAL OF BIOLOGICAL SYSTEMS,13(3),299-312.
MLA Ma, F,et al."Phylogenetic analysis of Na+/K+ ATPase: Insight into the mechanism for the genesis of multi-isoforms of protein complex".JOURNAL OF BIOLOGICAL SYSTEMS 13.3(2005):299-312.
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