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TitleStructural insight into H4K20 methylation on H2A.Z-nucleosome by SUV420H1.
Journal, issue, pagesMol Cell, Vol. 83, Issue 16, Page 2884-22895.e7, Year 2023
Publish dateAug 17, 2023
AuthorsLi Huang / Youwang Wang / Haizhen Long / Haoqiang Zhu / Zengqi Wen / Liwei Zhang / Wenhao Zhang / Zhenqian Guo / Longge Wang / Fangyi Tang / Jie Hu / Keyan Bao / Ping Zhu / Guohong Li / Zheng Zhou /
PubMed AbstractDNA replication ensures the accurate transmission of genetic information during the cell cycle. Histone variant H2A.Z is crucial for early replication origins licensing and activation in which ...DNA replication ensures the accurate transmission of genetic information during the cell cycle. Histone variant H2A.Z is crucial for early replication origins licensing and activation in which SUV420H1 preferentially recognizes H2A.Z-nucleosome and deposits H4 lysine 20 dimethylation (H4K20me2) on replication origins. Here, we report the cryo-EM structures of SUV420H1 bound to H2A.Z-nucleosome or H2A-nucleosome and demonstrate that SUV420H1 directly interacts with H4 N-terminal tail, the DNA, and the acidic patch in the nucleosome. The H4 (1-24) forms a lasso-shaped structure that stabilizes the SUV420H1-nucleosome complex and precisely projects the H4K20 residue into the SUV420H1 catalytic center. In vitro and in vivo analyses reveal a crucial role of the SUV420H1 KR loop (residues 214-223), which lies close to the H2A.Z-specific residues D97/S98, in H2A.Z-nucleosome preferential recognition. Together, our findings elucidate how SUV420H1 recognizes nucleosomes to ensure site-specific H4K20me2 modification and provide insights into how SUV420H1 preferentially recognizes H2A.Z nucleosome.
External linksMol Cell / PubMed:37536340
MethodsEM (single particle)
Resolution3.2 - 6.5 Å
Structure data

34053

7yrd

EMDB-34053, PDB-7yrd:
histone methyltransferase
Method: EM (single particle) / Resolution: 3.2 Å

34055

7yrg

EMDB-34055, PDB-7yrg:
histone methyltransferase
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-34056: histone methyltransferase
Method: EM (single particle) / Resolution: 5.1 Å

EMDB-34057: histone methyltransferase
Method: EM (single particle) / Resolution: 6.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SAM:
S-ADENOSYLMETHIONINE / S-Adenosyl methionine

Source
  • homo sapiens (human)
  • xenopus laevis (African clawed frog)
KeywordsGENE REGULATION / histone methyltransferase

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