Methylases

Ribozymes that use the cellular cofactor S-adenosyl-l-methionine to methylate RNA remained elusive. Now, such a ribozyme is reported by identifying natural sequences that are active in vitro; and crystal structures of the ribozyme with and without the cofactor are determined.

Schuhmacher, Beldar et al. design a super-substrate peptide based on the substrate sequence specificity of the SETD2 protein lysine methyltransferase. SETD2 methylates this super-substrate 290-fold more efficiently than the original H3K36 peptide. This study illustrates that substrate sequence design can improve the activity of protein lysine methyltransferases.

Husmann and Gozani review the biochemical and biological activities of histone lysine methyltransferases and their connections to human diseases, focusing on cancer.