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TitleCatalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1.
Journal, issue, pagesMol Cell, Vol. 83, Issue 16, Page 2872-22883.e7, Year 2023
Publish dateAug 17, 2023
AuthorsStephen Abini-Agbomson / Kristjan Gretarsson / Rochelle M Shih / Laura Hsieh / Tracy Lou / Pablo De Ioannes / Nikita Vasilyev / Rachel Lee / Miao Wang / Matthew D Simon / Jean-Paul Armache / Evgeny Nudler / Geeta Narlikar / Shixin Liu / Chao Lu / Karim-Jean Armache /
PubMed AbstractSUV420H1 di- and tri-methylates histone H4 lysine 20 (H4K20me2/H4K20me3) and plays crucial roles in DNA replication, repair, and heterochromatin formation. It is dysregulated in several cancers. Many ...SUV420H1 di- and tri-methylates histone H4 lysine 20 (H4K20me2/H4K20me3) and plays crucial roles in DNA replication, repair, and heterochromatin formation. It is dysregulated in several cancers. Many of these processes were linked to its catalytic activity. However, deletion and inhibition of SUV420H1 have shown distinct phenotypes, suggesting that the enzyme likely has uncharacterized non-catalytic activities. Our cryoelectron microscopy (cryo-EM), biochemical, biophysical, and cellular analyses reveal how SUV420H1 recognizes its nucleosome substrates, and how histone variant H2A.Z stimulates its catalytic activity. SUV420H1 binding to nucleosomes causes a dramatic detachment of nucleosomal DNA from the histone octamer, which is a non-catalytic activity. We hypothesize that this regulates the accessibility of large macromolecular complexes to chromatin. We show that SUV420H1 can promote chromatin condensation, another non-catalytic activity that we speculate is needed for its heterochromatin functions. Together, our studies uncover and characterize the catalytic and non-catalytic mechanisms of SUV420H1, a key histone methyltransferase that plays an essential role in genomic stability.
External linksMol Cell / PubMed:37595555
MethodsEM (single particle)
Resolution2.6 - 3.37 Å
Structure data

41109

8t9f

EMDB-41109, PDB-8t9f:
Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1
Method: EM (single particle) / Resolution: 2.6 Å

41111

8t9h

EMDB-41111, PDB-8t9h:
Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1
Method: EM (single particle) / Resolution: 3.37 Å

EMDB-41113: Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1
Method: EM (single particle) / Resolution: 3.08 Å

EMDB-41259: Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1
Method: EM (single particle) / Resolution: 3.1 Å

41272

8thu

EMDB-41272, PDB-8thu:
Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-SAM:
S-ADENOSYLMETHIONINE

Source
  • xenopus laevis (African clawed frog)
  • homo sapiens (human)
  • escherichia coli 'bl21-gold(de3)plyss ag' (bacteria)
  • synthetic construct (others)
KeywordsGENE REGULATION / Chromatin / Histone H4 modification / Methyltransferase / GENE REGULATION/DNA / GENE REGULATION-DNA complex

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