Post-translational lysine methylation is well established as a regulator of histone activity; however, it is emerging that these modifications are also likely to play extensive roles outside of the histone code. Here we obtain new insights into non-histone lysine methylation and protein lysine methyltransferase (PKMT) activity by elucidating absolute stoichiometries of lysine methylation, using mass spectrometry and absolute quantification (AQUA), in wild-type and 5 PKMT gene deletion strains of Saccharomyces cerevisiae. By analyzing 8 sites of methylation in 3 non-histone proteins, elongation factor 1-α (EF1α), elongation factor 2 (EF2), and 60S ribosomal protein L42-A/B (Rpl42ab), we find that production of preferred methylation states on individual lysine residues is commonplace and likely occurs through processive PKMT activity, Class I PKMTs can be associated with processive methylation, lysine residues are selectively methylated by specific PKMTs, and lysine methylation exists over a broad range of stoichiometries.
View Article and Find Full Text PDFDirect links between proteomic and genomic/transcriptomic data are not frequently made, partly because of lack of appropriate bioinformatics tools. To help address this, we have developed the PG Nexus pipeline. The PG Nexus allows users to covisualize peptides in the context of genomes or genomic contigs, along with RNA-seq reads.
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