Jumonji domain-containing protein

From Proteopedia
Jump to navigation Jump to search

SEE ALSO Lysine-specific histone demethylase

Function

  • Jumonji domain-containing protein 2a (Jmjd2a) or KDM4A or Lysine-specific demethylase catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 producing the dimethylated form. Jmjd2a domains contain: N-terminal, catalytic core (residues 1-350), 2 TUDOR domains which recognize dimethylated Arg (residues 895-1011) , 2 PHD-type zinc fingers and C-terminal domain. Jmjd2a is Fe+2 and α-ketoglutarate dependent. Methylation of histones in the chromatin is involved in regulation of gene activity, chromatin structure and epigenetic memory[1].
  • Jumonji domain-containing protein 2b (Jmjd2b) or KDM4B and Jumonji domain-containing protein 2d (Jmjd2d) or KDM4D catalyze the demethylation of trimethylated histone H3 at lysine residues 9 producing the dimethylated form.
  • Jumonji domain-containing protein 3 (Jmjd3) or KDM6B and Jumonji domain-containing protein 2d (Jmjd2d) or KDM4D catalyze the demethylation of trimethylated histone H3 at lysine residues 27 producing the dimethylated form[2].
  • Jumonji domain-containing protein 5 (Jmjd5) or KDM8 and Jumonji domain-containing protein 6 (Jmjd6) function as histone demethylase and as a protein hydroxylase.

Disease

Jmjd6 serves as a receptor allowing the foot-and-mouth virus to infect cells[3].

Structural highlights

Jmjd2a uses and . An [4]. Water molecules shown as red spheres.

.

3D structures of jumonji domain-containing protein

Jumonji domain-containing protein 3D structures


Structure of human Jumonji domain-containing protein 2a catalytic domain complex with oxalylglycine, Fe+2 ion (orange), Zn+2 ion (grey) and histone H3 peptide (aqua) with trimethyllysine (magenta) (PDB code 2p5b).

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Chen Z, Zang J, Whetstine J, Hong X, Davrazou F, Kutateladze TG, Simpson M, Mao Q, Pan CH, Dai S, Hagman J, Hansen K, Shi Y, Zhang G. Structural insights into histone demethylation by JMJD2 family members. Cell. 2006 May 19;125(4):691-702. Epub 2006 May 4. PMID:16677698 doi:http://dx.doi.org/10.1016/j.cell.2006.04.024
  2. ↑ Canovas S, Cibelli JB, Ross PJ. Jumonji domain-containing protein 3 regulates histone 3 lysine 27 methylation during bovine preimplantation development. Proc Natl Acad Sci U S A. 2012 Feb 14;109(7):2400-5. doi:, 10.1073/pnas.1119112109. Epub 2012 Jan 30. PMID:22308433 doi:http://dx.doi.org/10.1073/pnas.1119112109
  3. ↑ Lawrence P, Rai D, Conderino JS, Uddowla S, Rieder E. Role of Jumonji C-domain containing protein 6 (JMJD6) in infectivity of foot-and-mouth disease virus. Virology. 2016 Feb 18;492:38-52. doi: 10.1016/j.virol.2016.02.005. PMID:26896934 doi:http://dx.doi.org/10.1016/j.virol.2016.02.005
  4. ↑ Chen Z, Zang J, Kappler J, Hong X, Crawford F, Wang Q, Lan F, Jiang C, Whetstine J, Dai S, Hansen K, Shi Y, Zhang G. Structural basis of the recognition of a methylated histone tail by JMJD2A. Proc Natl Acad Sci U S A. 2007 Jun 26;104(26):10818-23. Epub 2007 Jun 13. PMID:17567753

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=Jumonji_domain-containing_protein&oldid=3088147"