Methylation-dependent SUMOylation of the architectural transcription factor HMGA2

High mobility group A2 (HMGA2) is a chromatin-associated protein involved in the regulation of stem cell function, embryogenesis and cancer development. Although does not contain consensus SUMOylation site, it shown to be SUMOylated. In this study, we demonstrate that first lysine residue reported K66KAE motif HMGA2 can methylated vitro vivo by Set7/9 methyltransferase. By editing lysine, increased hydrophobicity resulting 6-N-methyl-lysine transforms sequence into SUMO motif. This post-translational dramatically increases subsequent site. Furthermore, similar putative methylation-dependent motifs are found number other chromatin factors, confirm site one such protein, Polyhomeotic complex 1 homolog (PHC1). Together, these results suggest crosstalk between methylation general mode for function.