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Crystal structure and functional analysis of JMJD5 indicate an alternate specificity and function

Paul A Del Rizzo1, Swathi Krishnan, Raymond C Trievel

  • 1Department of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA.

Molecular and Cellular Biology
|August 2, 2012
PubMed

Insights

JMJD5, also known as KDM8, does not demethylate histone H3K36me2 as previously thought. Structural and biochemical data suggest JMJD5 may function as a protein hydroxylase, independent of histone demethylation roles.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Epigenetics

Background:

  • JMJD5 (KDM8) is a Jumonji C (JmjC) protein linked to various biological processes, including cancer and development.
  • Previous studies suggested JMJD5 functions as a histone demethylase, specifically targeting H3K36me2 to regulate cell cycle genes.

Purpose of the Study:

  • To elucidate the structural and biochemical properties of the JMJD5 catalytic domain.
  • To investigate the enzymatic activity of JMJD5, particularly its role in histone demethylation.

Main Methods:

  • High-resolution crystal structure determination of the human JMJD5 catalytic domain.
  • Biochemical assays to assess demethylase activity on various histone methylation marks.

Main Results:

  • Crystal structures revealed a conserved JmjC β-barrel fold with a distinct active site cleft.
  • JMJD5 shares structural homology with hydroxylases like FIH-1 and JMJD6, but limited homology with lysine demethylases (KDMs).
  • Biochemical assays demonstrated no detectable demethylase activity of JMJD5 on H3K36me2 or other histone methyllysines.

Conclusions:

  • Contrary to prior reports, JMJD5 does not exhibit histone demethylase activity.
  • The structural and biochemical data suggest JMJD5 may function as a protein hydroxylase, playing roles beyond histone modification.

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