Structural basis of nucleosomal H4K20 methylation by methyltransferase SET8-Reference-Cited by-同舟云学术

Structural basis of nucleosomal H4K20 methylation by methyltransferase SET8

Published:2022-05-09 Issue:6 Volume:36 Page:
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:The FASEB Journal

Author:

Shi Liuxin¹²^ORCID,Huang Li¹,Long Haizhen¹,Song Aoqun¹²,Zhou Zheng¹²^ORCID

Affiliation:

1. National Laboratory of Biomacromolecules CAS Center for Excellence in Biomacromolecules Institute of Biophysics Chinese Academy of Sciences Beijing China

2. University of Chinese Academy of Sciences Beijing China

Funder

National Natural Science Foundation of China

National Key Research and Development Program of China

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.202101821R

Reference45 articles.

1. PR-Set7 Is a Nucleosome-Specific Methyltransferase that Modifies Lysine 20 of Histone H4 and Is Associated with Silent Chromatin

2. Purification and Functional Characterization of SET8, a Nucleosomal Histone H4-Lysine 20-Specific Methyltransferase

3. Coupling mitosis to DNA replication: The emerging role of the histone H4-lysine 20 methyltransferase PR-Set7

4. Histone H4K20 methylation mediated chromatin compaction threshold ensures genome integrity by limiting DNA replication licensing

5. The histone methyltransferase SET8 is required for S-phase progression

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