Technology Listings


Human PHF8 Protein

Application

Human plant homeodomain finger protein 8 (PHF8) for use in assays to identify drugs that modulate human activity of the enzyme or to engineer recombinant protein for use in such assays.

Key Benefits
  • Allows for the function of individual methyl marks to be identified.
  • Applications towards mental retardation, cleft lip or palate, and other congenital abnormalities.
Technical Summary

Jumonji-C (JmjC) domain-containing proteins catalyze histone demethylation via an oxidative pathway that requires the presence of Fe(II) and α-ketoglutarate as cofactors. The active removal of methyl groups from histones plays an essential role in gene regulation. These enzymes are involved in a range of cellular processes including DNA replication and repair as well as transcriptional activation and repression.

Emory researchers have isolated the N-terminal domain, including the plant homeodomain (PHD) and the catalytic domain, of PHF8, a histone demethylase found in mice and humans that is selective for mono- and di-methylated lysine residues. The protein contains different segments for both recognizing and removing opposing methyl groups. While the PHD binds Lys4-trimethylated histone 3 (H3K4me3), an alteration associated with transcriptional activation, the jumonji (catalytic) domain demethylates H3K9me2, a mechanism associated with transcriptional repression. The enzymes’ catalytic activity and substrate specificity is thereby enhanced through the simultaneous binding of multiple domains. The ability to distinguish the function of individual methyl marks could lead to a marked understanding of the language of the histone code.

Publication: Horton J, et al. Nature. 17:38-43. (2010).

Patent Information
Tech ID: 13008
Published: 1/14/2013
Category
Research Tools

Contact
Rajsekhar Guddneppanavar
Licensing Associate
Emory University
RGUDDNE@emory.edu

Inventor(s)
Xiaodong Cheng
John Horton

Keywords
Assay
Enzyme/Protein