PUBLICATION
Diversity and functional plasticity of eukaryotic selenoproteins: Identification and characterization of the SelJ family
- Authors
- Castellano, S., Lobanov, A.V., Chapple, C., Novoselov, S.V., Albrecht, M., Hua, D., Lescure, A., Lengauer, T., Krol, A., Gladyshev, V.N., and Guigo, R.
- ID
- ZDB-PUB-051107-16
- Date
- 2005
- Source
- Proc Natl Acad Sci U S A. 2002 102(45): 16188-16193 (Journal)
- Registered Authors
- Gladyshev, Vadim, Krol, Alain, Lescure, Alain
- Keywords
- ADP-ribosylation, J1-crystallins, selenocysteine, selenium
- MeSH Terms
-
- Adenosine Diphosphate Ribose/metabolism
- Animals
- Fish Proteins/chemistry
- Fish Proteins/genetics
- Fish Proteins/physiology*
- Genome
- Mice
- NIH 3T3 Cells
- Phylogeny
- Promoter Regions, Genetic
- Proteome
- Selenoproteins/chemistry
- Selenoproteins/genetics
- Selenoproteins/physiology*
- Tetraodontiformes/genetics*
- PubMed
- 16260744 Full text @ Proc Natl Acad Sci U S A. 2002
Citation
Castellano, S., Lobanov, A.V., Chapple, C., Novoselov, S.V., Albrecht, M., Hua, D., Lescure, A., Lengauer, T., Krol, A., Gladyshev, V.N., and Guigo, R. (2005) Diversity and functional plasticity of eukaryotic selenoproteins: Identification and characterization of the SelJ family. Proc Natl Acad Sci U S A. 2002. 102(45):16188-16193.
Abstract
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping