Kansl2 dependent acetylome study in primary Kansl2 (fl/fl) murine embryonic fibroblasts

As one of the most important post-translational protein modifications, lysine acetylation is catalyzed by lysine acetyltransferases (KATs), which catalyze the covalent attachment of an acetyl group to the N epsilon–residue of lysine. The histone acetyltransferase MOF, which represents the main histone H4 lysine-16 specific acetyltransferase, is the KAT subunit of two mutually exclusive multiprotein complexes in metazoa, namely the MSL (male-specific lethal) and the NSL (non-specific lethal) complex. Depletion of both, MOF and the NSL complex subunit Kansl2 result in selective changes of the cellular acetylome. As a consequence, modulation of nuclear lamin lysine acetylations correlate with profound changes in nuclear morphology, like micronuclei formation.