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.

Genetic and molecular analyses identify and characterize an evolutionary battle over lysis timing wherein a bacteriophage delays lysis through lysis inhibition while a defensive phage satellite accelerates lysis.

The first recently discovered inhibitors of lysine biosynthesis with in planta activity have a dual-target mode of action, which provides proof-of-concept for the development of multi-target ‘resistance-resistant’ herbicides with a novel mode of action.

Proof-of-principle for a new herbicide mode of action through the identification of novel inhibitors of lysine biosynthesis with in planta efficacy.

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

Structural studies reveal the mechanism by which a HECT E3 ubiquitin ligase carries out E2-to-E3-to-substrate ubiquitin transfer and prioritizes target lysines for ubiquitination.

Sirt3 functions as decrotonylase to regulate histone crotonylation dynamics.

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.

Origin recognition complex-associated (ORCA) is crucial for the stability of the Histone H3 lysine 9 methyltransferase megacomplex, which is essential for heterochromatin organization.