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A proteomic approach for the identification of novel lysine methyltransferase substrates

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Author(s): Levy Dan | Liu Chih Long | Yang Ze | Newman Aaron M | Alizadeh Ash A | Utz Paul J | Gozani Or

Journal: Epigenetics & Chromatin
ISSN 1756-8935

Volume: 4;
Issue: 1;
Start page: 19;
Date: 2011;
Original page

ABSTRACT
Abstract Background Signaling via protein lysine methylation has been proposed to play a central role in the regulation of many physiologic and pathologic programs. In contrast to other post-translational modifications such as phosphorylation, proteome-wide approaches to investigate lysine methylation networks do not exist. Results In the current study, we used the ProtoArray® platform, containing over 9,500 human proteins, and developed and optimized a system for proteome-wide identification of novel methylation events catalyzed by the protein lysine methyltransferase (PKMT) SETD6. This enzyme had previously been shown to methylate the transcription factor RelA, but it was not known whether SETD6 had other substrates. By using two independent detection approaches, we identified novel candidate substrates for SETD6, and verified that all targets tested in vitro and in cells were genuine substrates. Conclusions We describe a novel proteome-wide methodology for the identification of new PKMT substrates. This technological advance may lead to a better understanding of the enzymatic activity and substrate specificity of the large number (more than 50) PKMTs present in the human proteome, most of which are uncharacterized.

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