Clipping of arginine-methylated histone tails by JMJD5 and JMJD7.


Journal Article

Two of the unsolved, important questions about epigenetics are: do histone arginine demethylases exist, and is the removal of histone tails by proteolysis a major epigenetic modification process? Here, we report that two orphan Jumonji C domain (JmjC)-containing proteins, JMJD5 and JMJD7, have divalent cation-dependent protease activities that preferentially cleave the tails of histones 2, 3, or 4 containing methylated arginines. After the initial specific cleavage, JMJD5 and JMJD7, acting as aminopeptidases, progressively digest the C-terminal products. JMJD5-deficient fibroblasts exhibit dramatically increased levels of methylated arginines and histones. Furthermore, depletion of JMJD7 in breast cancer cells greatly decreases cell proliferation. The protease activities of JMJD5 and JMJD7 represent a mechanism for removal of histone tails bearing methylated arginine residues and define a potential mechanism of transcription regulation.

Full Text

Duke Authors

Cited Authors

  • Liu, H; Wang, C; Lee, S; Deng, Y; Wither, M; Oh, S; Ning, F; Dege, C; Zhang, Q; Liu, X; Johnson, AM; Zang, J; Chen, Z; Janknecht, R; Hansen, K; Marrack, P; Li, C-Y; Kappler, JW; Hagman, J; Zhang, G

Published Date

  • September 12, 2017

Published In

Volume / Issue

  • 114 / 37

Start / End Page

  • E7717 - E7726

PubMed ID

  • 28847961

Pubmed Central ID

  • 28847961

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

Digital Object Identifier (DOI)

  • 10.1073/pnas.1706831114


  • eng

Conference Location

  • United States