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Enzyme
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Target Concepts:
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Query: UNIPROT:P36969 (
phospholipid hydroperoxide glutathione peroxidase
)
344
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
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.
...
PMID:Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtii. 1211 May 81