PUBLICATION

Composition and Evolution of the Vertebrate and Mammalian Selenoproteomes

Authors
Mariotti, M., Ridge, P.G., Zhang, Y., Lobanov, A.V., Pringle, T.H., Guigo, R., Hatfield, D.L., Gladyshev, V.N.
ID
ZDB-PUB-170927-1
Date
2012
Source
PLoS One   7(3): e33066 (Journal)
Registered Authors
Gladyshev, Vadim, Hatfield, Dolph L.
Keywords
Vertebrates, Sequence alignment, Mammals, Pseudogenes, Phylogenetic analysis, Multiple alignment calculation, Gene expression, Osteichthyes
MeSH Terms
  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Evolution, Molecular
  • Gene Duplication
  • Humans
  • Mammals/genetics
  • Mammals/metabolism*
  • Molecular Sequence Data
  • Mutation
  • Phylogeny
  • Protein Isoforms/classification
  • Protein Isoforms/genetics
  • Protein Isoforms/metabolism
  • Proteome/classification
  • Proteome/genetics
  • Proteome/metabolism*
  • Proteomics
  • Pseudogenes/genetics
  • Selenoproteins/classification
  • Selenoproteins/genetics
  • Selenoproteins/metabolism*
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Vertebrates/genetics
  • Vertebrates/metabolism*
PubMed
22479358 Full text @ PLoS One
Abstract

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.

Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping