The acetylation of histones at specific sites close to DNA can regulate transcription.

A new post-translational regulatory mechanism of K-Ras is identified, which expands the function of reversible protein lysine fatty acylation and offers new possibility to target the K-Ras oncoprotein.

Biochemical approaches reveal that an epigenetic histone deacetylase complex called CoREST is slow to deacetylate histone H3 lysine-14 in nucleosomes, and this inhibits demethylation of histone H3 lysine-4 by the CoREST complex.

We applied a combined synthetic biological, biochemical and mass-spectrometric approach to show that YcgC is not a member of a novel lysine deacetylase class in prokaryotes.

Mass spectroscopy, molecular modeling and/or molecular dynamics simulations reveal how acetylation regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation.

A posttranslational regulatory mechanism for a Ras family small GTPase could open up new directions to understand and control the Ras family of proteins that are important for physiology and diseases.

Structural and biochemical studies of Kap123 revealed the mechanisms by which Kap123 recognizes H3- and H4-NLSs through two lysine-binding pockets and by which evolutionarily conserved diacetylation of H4-NLS facilitates Kap123-H3-NLS mediated nuclear translocation.

The lysine acetyltransferases KAT2A and KAT2B regulate the dynamic chromatin association of the tumour suppressor protein PALB2, protecting active genes and promoting DNA damage repair in a context-dependent manner.

A protein microarray based strategy has identified a bacterial enzyme that represents a new protein deacetylase family.

Lysine mono- and di-methylation are two novel post-translational modifications of RNA polymerase II, which are enriched at promoters of active genes, precede lysine acetylation and mark early stages of transcription.