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TitleThe structure of the NuA4-Tip60 complex reveals the mechanism and importance of long-range chromatin modification.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 9, Page 1337-1345, Year 2023
Publish dateAug 7, 2023
AuthorsAlexander Fréchard / Céline Faux / Rozalie Hexnerova / Corinne Crucifix / Gabor Papai / Ekaterina Smirnova / Conor McKeon / Florie Lo Ying Ping / Dominique Helmlinger / Patrick Schultz / Adam Ben-Shem /
PubMed AbstractHistone acetylation regulates most DNA transactions and is dynamically controlled by highly conserved enzymes. The only essential histone acetyltransferase (HAT) in yeast, Esa1, is part of the 1-MDa ...Histone acetylation regulates most DNA transactions and is dynamically controlled by highly conserved enzymes. The only essential histone acetyltransferase (HAT) in yeast, Esa1, is part of the 1-MDa NuA4 complex, which plays pivotal roles in both transcription and DNA-damage repair. NuA4 has the unique capacity to acetylate histone targets located several nucleosomes away from its recruitment site. Neither the molecular mechanism of this activity nor its physiological importance are known. Here we report the structure of the Pichia pastoris NuA4 complex, with its core resolved at 3.4-Å resolution. Three subunits, Epl1, Eaf1 and Swc4, intertwine to form a stable platform that coordinates all other modules. The HAT module is firmly anchored into the core while retaining the ability to stretch out over a long distance. We provide structural, biochemical and genetic evidence that an unfolded linker region of the Epl1 subunit is critical for this long-range activity. Specifically, shortening the Epl1 linker causes severe growth defects and reduced H4 acetylation levels over broad chromatin regions in fission yeast. Our work lays the foundations for a mechanistic understanding of NuA4's regulatory role and elucidates how its essential long-range activity is attained.
External linksNat Struct Mol Biol / PubMed:37550452
MethodsEM (single particle)
Resolution3.34 - 3.9 Å
Structure data

EMDB-14980: NuA4 Histone Acetyltransferase complex
Method: EM (single particle) / Resolution: 3.7 Å

14989

7zvw

EMDB-14989: NuA4 Histone Acetyltransferase Complex (Composite)
PDB-7zvw: NuA4 Histone Acetyltransferase Complex
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-15066: NuA4 Histone Acetyltransferase complex - Upper lobe
Method: EM (single particle) / Resolution: 3.34 Å

EMDB-15067: NuA4 Histone Acetyltransferase complex - Tra1 part 1
Method: EM (single particle) / Resolution: 3.36 Å

EMDB-15070: NuA4 Histone Acetyltransferase complex - Tra1 Part 2
Method: EM (single particle) / Resolution: 3.41 Å

EMDB-15869: NuA4 Histone Acetyltransferase Complex Epl1 full length
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-15881: NuA4 Histone Acetyltransferase Complex Full length Epl1 Core
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-15896: NuA4 Histone Acetyltransferase Complex Shortened Epl1 Loop 1 (SL1)
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-15897: NuA4 Histone Acetyltransferase Complex Epl1 Shortened Loop 1 (SL1) core
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • komagataella phaffii gs115 (fungus)
KeywordsTRANSCRIPTION / NuA4 / histone acetyltransferase complex / Epigenetics / DNA repair

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