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Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

Proteomics.. 2016-02;  16(3):465-76
Jason K. K. Low, Hogune Im, Melissa A. Erce, Gene Hart-Smith, Michael P. Snyder, Marc R. Wilkins. Professor Marc R. Wilkins, Systems Biology Initiative, School of Biotechnology and Biomolecular Sciences, The University of New South Wales, NSW 2052, Sydney, Australia.
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摘要

Arginine methylation on nonhistone proteins is associated with a number of cellular processes including RNA splicing, protein localization, and the formation of protein complexes. In this manuscript, Saccharomyces cerevisiae proteome arrays carrying 4228 proteins were used with an antimethylarginine antibody to first identify 88 putatively arginine-methylated proteins. By treating the arrays with recombinant arginine methyltransferase Hmt1, 42 proteins were found to be possible substrates of this enzyme. Analysis of the putative arginine-methylated proteins revealed that they were predominantly nuclear or nucleolar in localization, consistent with the localization of Hmt1. Many are involved in known methylargin... More

关键词

Arginine methylation; Hmt1 methyltransferase; Post-translational modification; Proteome arrays; Saccharomyces cerevisiae