In particular, dimethylation and trimethylation of lysine side chains in proteins increase both hydrophobicity and steric bulk and can affect protein¨Cprotein interactions if they are in an interacting surface.

Reference
Wiki: Trimethylation

    During the transportation from the cytosol, then the nucleus, and then to incorporate new chromatin at the replication fork, histones receive more modifications like monomethylation of lysine 9.

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Wiki: Monomethylation

    Methylation, in the chemical sciences, is the addition of a methyl group on a substrate, or the substitution of an atom (or group) by a methyl group. Methylation is a form of alkylation, with a methyl group replacing a hydrogen atom. These terms are commonly used in chemistry, biochemistry, soil science, and biology. In biological systems, methylation is catalyzed by enzymes; such methylation can be involved in modification of heavy metals, regulation of gene expression, regulation of protein function, and RNA processing. In vitro methylation of tissue samples is also a way to reduce some histological staining artifacts. The reverse of methylation is demethylation.

Reference
Wiki: Methylation

    Protein lysine methylation, is a PTM involving the transfer of one, two or three methyl groups to the epsilon - amine of a lysine side chain. Lysine methylation represents a complex and often elusive PTM that has nonetheless the potential to alter the function of the modified protein. lysine methylation has been observed in both nuclear and cytoplasmic proteins and is now considered a prevalent modification in eukaryotes, prokaryotes and archaea. Two groups of enzymes, both using S - adenosyl - L - methionine (SAM) as a methyl donor, catalyze the addition of a methyl group to the epsilon - amine group of a lysine side chain. The first type of protein lysine methyltransferase regroups the enzymes containing a catalytic SET domain and the second class of PKMTs, the seven beta - strand methyltransferases (class I methyltransferases), belongs to an extended superfamily of methyltransferases found throughout eukaryotes, prokaryotes and archaea.

Reference
Wiki: Lysine methylation

    Methylation on leucine was first observed in 1999, the carboxyl methyltransferase, which is claimed to exclusively methylate the carboxyl group of the C-terminal leucine residue of the catalytic subunit of protein phosphatase 2A (Leu(309)), was purified from porcine brain. The cDNA encoding the human homologue was also cloned. The cDNA of this gene encodes for a protein of 334 amino acids with a calculated M(r) of 38 305 and a predicted pI of 5.72. Database screening reveals the presence of this protein in diverse phyla. Recent studies revealed that PP2A methylation is associated with "PP2A" dysfunction which has been linked to tau hyperphosphorylation, amyloidogenesis and synaptic deficits that are pathological hallmarks of this neurodegenerative disorder.

Reference
Wiki: Leucine methylation

    In particular, dimethylation and trimethylation of lysine side chains in proteins increase both hydrophobicity and steric bulk and can affect protein¨Cprotein interactions if they are in an interacting surface.

Reference
Wiki: Dimethylation

    Demethylation is the chemical process resulting in the removal of a methyl group (CH3) from a molecule. A common way of demethylation is the replacement of a methyl group by a hydrogen atom, resulting in a net loss of one carbon and two hydrogen atoms. The counterpart of demethylation is methylation.

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Wiki: Demethylation

    The Metnase SET domain is not only responsible for dimethylation of H3K36 but also crucial for automethylation at K485 within the catalytic pocket.

Reference
Pubmed: Kim HS, Kim SK, Hromas R, Lee SH. The SET Domain Is Essential for Metnase Functions in Replication Restart and the 5' End of SS-Overhang Cleavage. PLoS One. 2015 Oct 5;10(10):e0139418. doi: 10.1371/journal.pone.0139418.

    Arginine methylation is a prevalent post-translational modification found on both nuclear and cytoplasmic proteins. The methylation of arginine residues is catalyzed by the protein arginine Nmethyltransferase (PRMT) family of enzymes. Proteins that are arginine methylated are involved in a number of different cellular processes, including transcriptional regulation, RNA metabolism and DNA damage repair (Bedford and Richard, 2005). Most PRMTs methylate glycine- and arginine-rich patches (GAR motifs) within their substrates.

Reference
Wiki: Arginine methylation