Specific Recognition of Arginine Methylated Histone Tails by JMJD5 and JMJD7

Liu, Haolin; Wang, Chao; Lee, Schuyler; Ning, Fangkun; Wang, Yang; Zhang, Qianqian; Chen, Zhongzhou; Zang, Jianye; Nix, Jay; Dai, Shaodong; Marrack, Philippa; Hagman, James; Kappler, John; Zhang, Gongyi

doi:10.1038/s41598-018-21432-8

Title: Specific Recognition of Arginine Methylated Histone Tails by JMJD5 and JMJD7

Journal Article · Mon Feb 19 00:00:00 EST 2018 · Scientific Reports

DOI:https://doi.org/10.1038/s41598-018-21432-8· OSTI ID:1560549

Liu, Haolin ^[1]; Wang, Chao ^[2]; Lee, Schuyler ^[2]; Ning, Fangkun ^[2]; Wang, Yang ^[2]; Zhang, Qianqian ^[3];

^[3]; Zang, Jianye ^[4]; Nix, Jay ^[5]; Dai, Shaodong ^[2]; Marrack, Philippa ^[1];

^[2]; Kappler, John ^[1]; Zhang, Gongyi ^[2]

National Jewish Health, Denver, CO (United States); Univ. of Colorado, Denver, CO (United States); Howard Hughes Medical Institute, Denver, CO (United States)
National Jewish Health, Denver, CO (United States); Univ. of Colorado, Denver, CO (United States)
Chinese Agricultural Univ., Beijing (China)
Univ. of Science and Technology of China, Hefei (China)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)

We have reported that JMJD5 and JMJD7 (JMJD5/7) are responsible for the clipping of arginine methylated histone tails to generate "tailless nucleosomes", which could release the pausing RNA polymerase II (Pol II) into productive transcription elongation. JMJD5/7 function as endopeptidases that cleave histone tails specifically adjacent to methylated arginine residues and continue to degrade N-terminal residues of histones via their aminopeptidase activity. Here, we report structural and biochemical studies on JMJD5/7 to understand the basis of substrate recognition and catalysis mechanism by this JmjC subfamily. Recognition between these enzymes and histone substrates is specific, which is reflected by the binding data between enzymes and substrates. High structural similarity between JMJD5 and JMJD7 is reflected by the shared common substrates and high binding affinity. However, JMJD5 does not bind to arginine methylated histone tails with additional lysine acetylation while JMJD7 does not bind to arginine methylated histone tails with additional lysine methylation. Furthermore, the complex structures of JMJD5 and arginine derivatives revealed a Tudor domain-like binding pocket to accommodate the methylated sidechain of arginine, but not lysine. There also exists a glutamine close to the catalytic center, which may suggest a unique imidic acid mediated catalytic mechanism for proteolysis by JMJD5/7.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1560549

Journal Information:: Scientific Reports, Vol. 8, Issue 1; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 16 works

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