Molecular biology experiments identified a cleaved METTL3, which mediates the METTL3–METTL3 interaction, a prerequisite step for recruitment of WTAP in MTC assembly, controlling m6A deposition and cancer progression.

Elucidating the molecular mechanism by which the Hippo signaling effector Yorkie (Yki) functions as a transcriptional coactivator in growth control reveals the importance of a histone-modifying enzyme for this process.

A zebrafish model for a particular form of human deafness (DFNB63) changes our view of this disease by revealing a defect in the localization of Transmembrane channel-like proteins that are essential for mechanotransduction in sensory cells.

The SARS-CoV-2 main protease specifically cleaves a conserved sequence in the human tRNA modifying enzyme TRMT1, resulting in reduced tRNA binding and the complete loss of TRMT1-mediated tRNA methyltransferase activity.

The structure of the catalytic core of the N6-methyladenosine RNA methyltransferase complex METTL3-METTL14 reveals that METTL3 is the catalytic subunit, while METTL14 plays non-catalytic roles in substrate recognition and in maintaining complex integrity.

Structured RNA elements bind to the human methyltransferase like-3 (METTL3)-METTL14 enzyme complex with high affinity and restrict the formation of N⁶-deoxymethyladenosine in DNA.

Clr4, a highly conserved SUV39 histone methyltransferase, requires its SET domain to sense histone H3K14 ubiquitination in order to maintain heterochromatin and H3K9 methylation.

A lysine-to-methionine mutation in histone H3 dominantly blocks histone H3K9 methylation by trapping its methyltransferase.

The N6-methyladenosine (m6A) methyltransferase complex in budding yeast is highly conserved, yet reconfigured with respect to its mammalian counterpart and has both m6A-dependent and m6A-independent functions.

A viral protein hijacks the key effector of transcriptional gene silencing, Su(var)3-9, to evade host plant surveillance.