Diversity and functional plasticity of eukaryotic selenoproteins: Identification and characterization of the SelJ family
| Autor: | Alain Krol, Deame Hua, Mario Albrecht, Sergey V. Novoselov, Vadim N. Gladyshev, Alain Lescure, Charles Chapple, Sergi Castellano, Thomas Lengauer, Roderic Guigó, Alexey V. Lobanov |
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| Rok vydání: | 2005 |
| Předmět: |
Fish Proteins
Subfamily Proteome Biology Genome Mice chemistry.chemical_compound Phylogenetics Crystallin Animals Promoter Regions Genetic Selenoproteins Gene Phylogeny Genetics chemistry.chemical_classification Adenosine Diphosphate Ribose Multidisciplinary integumentary system Selenocysteine Tetraodontiformes Biological Sciences Genetic code Biological Evolution chemistry Evolutionary biology NIH 3T3 Cells Commentary Selenoprotein |
| Zdroj: | Proceedings of the National Academy of Sciences. 102:16188-16193 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.0505146102 |
| Popis: | Selenoproteins are a diverse group of proteins that contain selenocysteine (Sec), the 21st amino acid. In the genetic code, UGA serves as a termination signal and a Sec codon. This dual role has precluded the automatic annotation of selenoproteins. Recent advances in the computational identification of selenoprotein genes have provided a first glimpse of the size, functions, and phylogenetic diversity of eukaryotic selenoproteomes. Here, we describe the identification of a selenoprotein family named SelJ. In contrast to known selenoproteins, SelJ appears to be restricted to actinopterygian fishes and sea urchin, with Cys homologues only found in cnidarians. SelJ shows significant similarity to the jellyfish J1-crystallins and with them constitutes a distinct subfamily within the large family of ADP-ribosylation enzymes. Consistent with its potential role as a structural crystallin, SelJ has preferential and homogeneous expression in the eye lens in early stages of zebrafish development. A structural role for SelJ would be in contrast to the majority of known selenoenzymes. The unusually highly restricted phylogenetic distribution of SelJ, its specialization, and the comparative analysis of eukaryotic selenoproteomes reveal the diversity and functional plasticity of selenoproteins and point to a mosaic evolution of the use of Sec in proteins. |
| Databáze: | OpenAIRE |
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