G9a-like protein

From WikiMD's Wellness Encyclopedia

G9a-like Protein[edit | edit source]

G9a-like protein, also known as EHMT2 (Euchromatic Histone Lysine Methyltransferase 2), is a crucial enzyme involved in the epigenetic regulation of gene expression. It is a member of the SET domain-containing family of histone methyltransferases, which specifically methylate lysine residues on histone proteins, thereby influencing chromatin structure and gene activity.

Structure[edit | edit source]

G9a-like protein is characterized by the presence of a SET domain, which is responsible for its methyltransferase activity. The protein also contains other domains such as the ankyrin repeat domain, which is involved in protein-protein interactions. The structure of G9a-like protein allows it to interact with various substrates and cofactors, facilitating its role in chromatin modification.

Function[edit | edit source]

The primary function of G9a-like protein is to catalyze the mono- and dimethylation of histone H3 at lysine 9 (H3K9me1 and H3K9me2). This modification is associated with transcriptional repression and the formation of heterochromatin. G9a-like protein plays a significant role in:

  • Gene silencing: By methylating H3K9, G9a-like protein contributes to the repression of gene expression, particularly in euchromatic regions.
  • Embryonic development: It is essential for proper development, as it regulates the expression of genes involved in differentiation and growth.
  • Cancer: Aberrant expression or mutation of G9a-like protein has been implicated in various cancers, where it may contribute to the silencing of tumor suppressor genes.

Clinical Significance[edit | edit source]

G9a-like protein is a potential target for therapeutic intervention in diseases where epigenetic dysregulation plays a role. Inhibitors of G9a-like protein are being explored for their potential to reactivate silenced genes in cancer and other diseases.

Research and Development[edit | edit source]

Ongoing research is focused on understanding the precise mechanisms by which G9a-like protein regulates gene expression and its interactions with other epigenetic modifiers. Studies are also investigating the development of specific inhibitors that can modulate its activity for therapeutic purposes.

See Also[edit | edit source]

References[edit | edit source]

  • Tachibana, M., et al. (2002). "G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis." Genes & Development, 16(14), 1779-1791.
  • Shinkai, Y., & Tachibana, M. (2011). "H3K9 methyltransferase G9a and the related molecule GLP." Genes & Development, 25(8), 781-788.
WikiMD
Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD

Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD

WikiMD's Wellness Encyclopedia

Let Food Be Thy Medicine
Medicine Thy Food - Hippocrates

Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.

Contributors: Prab R. Tumpati, MD