Readers of histone methylarginine marks

Area of Science:

• Biochemistry
• Molecular Biology
• Epigenetics

Background:

• Arginine methylation is a prevalent posttranslational modification (PTM) affecting approximately 0.5% of cellular arginine residues.
• Three main types exist: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA), and symmetric dimethylarginine (SDMA).
• These modifications are notably found on RNA-binding proteins and histones, influencing signal transduction pathways.

Purpose of the Study:

• To review the biological significance of arginine methylation.
• To highlight the roles of Tudor domain-containing proteins in recognizing methylarginine marks.
• To discuss other interactions regulated by these PTMs.

Main Methods:

• Literature review focusing on arginine methylation and Tudor domain interactions.
• Analysis of existing data on methylarginine sites in core histones.
• Examination of the functional characterization of Tudor domain proteins.

Main Results:

• Over thirty arginine methylation sites have been identified on core histones.
• Arginine methylation alters protein structure, DNA interactions, and creates docking sites for effector molecules.
• At least ten Tudor domains bind methyllysine, and eight bind methylarginine motifs.

Conclusions:

• Tudor domains are critical readers of methylarginine marks, mediating diverse biological functions.
• Understanding these interactions is key to deciphering histone modification mechanisms.
• Arginine methylation plays a significant role in regulating protein function and cellular processes.