A proteomic approach for the identification of novel lysine methyltransferase substrates.

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 nove

SUBMITTER: Levy D 

PROVIDER: S-EPMC3212905 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature