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- Title
Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtii.
- Authors
Novoselov, Sergey V; Rao, Mahadev; Onoshko, Natalia V; Zhi, Huijun; Kryukov, Gregory V; Xiang, Youbin; Weeks, Donald P; Hatfield, Dolph L; Gladyshev, Vadim N
- Abstract
Known eukaryotic selenocysteine (Sec)-containing proteins are animal proteins, whereas selenoproteins have not been found in yeast and plants. Surprisingly, we detected selenoproteins in a member of the plant kingdom, Chlamydomonas reinhardtii, and directly identified two of them as phospholipid hydroperoxide glutathione peroxidase and selenoprotein W homologs. Moreover, a selenocysteyl-tRNA was isolated that recognized specifically the Sec codon UGA. Subsequent gene cloning and bioinformatics analyses identified eight additional selenoproteins, including methionine-S-sulfoxide reductase, a selenoprotein specific to Chlamydomonas: Chlamydomonas selenoprotein genes contained selenocysteine insertion sequence (SECIS) elements that were similar, but not identical, to those of animals. These SECIS elements could direct selenoprotein synthesis in mammalian cells, indicating a common origin of plant and animal Sec insertion systems. We found that selenium is required for optimal growth of Chlamydomonas: Finally, evolutionary analyses suggested that selenoproteins present in Chlamydomonas and animals evolved early, and were independently lost in land plants, yeast and some animals.
- Publication
The EMBO journal, 2002, Vol 21, Issue 14, p3681
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/cdf372