| Literature DB >> 28847961 |
Haolin Liu1,2,3, Chao Wang1,2, Schuyler Lee1,2, Yu Deng4, Matthew Wither5, Sangphil Oh6, Fangkun Ning1,2, Carissa Dege1,2, Qianqian Zhang7, Xinjian Liu4, Aaron M Johnson5, Jianye Zang8, Zhongzhou Chen7, Ralf Janknecht6, Kirk Hansen5, Philippa Marrack1,2,3,5, Chuan-Yuan Li4, John W Kappler9,2,3, James Hagman9,2,5, Gongyi Zhang9,2.
Abstract
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.Entities:
Keywords: JMJD5/7; arginine methylation; clipping; histone tail
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Year: 2017 PMID： 28847961 PMCID： PMC5604019 DOI： 10.1073/pnas.1706831114
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205