The lysine multi-switch: the impact of lysine methylation on transcription factor properties

The amino acid lysine can undergo methylation, acylation, sumoylation or ubiquitination, making it an extremely versatile protein residue. Its involvement in the modulation of protein biological functions through de/methylation on histones has been well studied but only recently has the focus shifted towards this post-translational modification in non-histone proteins particularly transcription factors. Lysine methylation has been found to act as a switch which can directly alter function or stability, as well as indirectly alter binding affinity to target DNA motifs and protein partners. Lysine methylation has been best-studied in the tumour suppressor p53, making it the ideal transcription factor to showcase how these different mechanisms act. Other transcription factors that undergo such a post-translational modification include NFkB, STAT3 and TFIID.Review | Biohelikon : Cell Biolog