Composition and Evolution of the Vertebrate and Mammalian Selenoproteomes
| Autor: | Yan Zhang, Roderic Guigó, Alexei V. Lobanov, Dolph L. Hatfield, Vadim N. Gladyshev, Thomas H. Pringle, Marco Mariotti, Perry G. Ridge |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Proteomics
Genome evolution Proteome Pseudogene Gene prediction Molecular Sequence Data lcsh:Medicine Biology Biochemistry Evolution Molecular biology.animal Gene Duplication Sequence Homology Nucleic Acid Gene duplication Animals Humans Protein Isoforms Amino Acid Sequence lcsh:Science Selenoproteins Phylogeny Genetics chemistry.chemical_classification Mammals Evolutionary Biology Multidisciplinary Base Sequence Sequence Homology Amino Acid Mamífers -- Metabolisme Alternative splicing lcsh:R Vertebrate Proteins Computational Biology Selenoprotein T Genomics Alternative Splicing chemistry Mutation Vertebrates lcsh:Q Selenoprotein Proteïnes Zoology Pseudogenes Vertebrats -- Metabolisme Research Article |
| Zdroj: | PLoS ONE PLoS ONE, Vol 7, Iss 3, p e33066 (2012) Recercat. Dipósit de la Recerca de Catalunya instname |
| ISSN: | 1932-6203 |
| Popis: | BACKGROUND: Selenium is an essential trace element in mammals due to its presence in proteins in the form of selenocysteine (Sec). Human genome codes for 25 Sec-containing protein genes, and mouse and rat genomes for 24. METHODOLOGY/PRINCIPAL FINDINGS: We characterized the selenoproteomes of 44 sequenced vertebrates by applying gene prediction and phylogenetic reconstruction methods, supplemented with the analyses of gene structures, alternative splicing isoforms, untranslated regions, SECIS elements, and pseudogenes. In total, we detected 45 selenoprotein subfamilies. 28 of them were found in mammals, and 41 in bony fishes. We define the ancestral vertebrate (28 proteins) and mammalian (25 proteins) selenoproteomes, and describe how they evolved along lineages through gene duplication (20 events), gene loss (10 events) and replacement of Sec with cysteine (12 events). We show that an intronless selenophosphate synthetase 2 gene evolved in early mammals and replaced functionally the original multiexon gene in placental mammals, whereas both genes remain in marsupials. Mammalian thioredoxin reductase 1 and thioredoxin-glutathione reductase evolved from an ancestral glutaredoxin-domain containing enzyme, still present in fish. Selenoprotein V and GPx6 evolved specifically in placental mammals from duplications of SelW and GPx3, respectively, and GPx6 lost Sec several times independently. Bony fishes were characterized by duplications of several selenoprotein families (GPx1, GPx3, GPx4, Dio3, MsrB1, SelJ, SelO, SelT, SelU1, and SelW2). Finally, we report identification of new isoforms for several selenoproteins and describe unusually conserved selenoprotein pseudogenes. CONCLUSIONS/SIGNIFICANCE: This analysis represents the first comprehensive survey of the vertebrate and mammal selenoproteomes, and depicts their evolution along lineages. It also provides a wealth of information on these selenoproteins and their forms. Supported by NIH GM061603 and GM065204 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|