Journal
FEBS JOURNAL
Volume 279, Issue 6, Pages 932-945Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1742-4658.2012.08490.x
Keywords
DART; histone code; model system; PRMT; protein arginine methylation
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Funding
- National Science Council of Republic of China [98-2320-B-040-011-MY3]
- Chung Shan Medical University [99-OM-A-128]
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Protein arginine methylation is catalyzed by members of the protein arginine methyltransferase (PRMT) family. In the present review, nine PRMTs identified in mammals (human) were used as templates to survey homologous PRMTs in 10 animal species with a completed sequence available in non-mammalian vertebrates, invertebrate chordates, echinoderms, arthropods, nematodes and cnidarians. We show the conservation of the most typical type I PRMT1 and type II PRMT5 in all of the species examined, the wide yet different distribution of PRMT3, 4 and 7 in non-mammalian animals, the vertebrate-restricted distribution of PRMT8 and the special reptile/avian-deficient distribution of PRMT2 and 6. We summarize the basic functions of each PRMT and focus on the current investigations of PRMTs in the non-mammalian animal models, including Xenopus, fish (zebrafish, flounder and medaka), Drosophila and Caenorhabditis elegans. Studies in the model systems not only complement the understanding of the functions of PRMTs in mammals, but also provide valuable information about their evolution, as well as their critical roles and interplays.
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