Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure of human TIP60-C histone exchange and acetyltransferase complex.
Journal, issue, pages	Nature, Year 2024
Publish date	Sep 11, 2024
Authors	Changqing Li / Ekaterina Smirnova / Charlotte Schnitzler / Corinne Crucifix / Jean Paul Concordet / Alice Brion / Arnaud Poterszman / Patrick Schultz / Gabor Papai / Adam Ben-Shem /
PubMed Abstract	Chromatin structure is a key regulator of DNA transcription, replication, and repair. In humans, the TIP60/EP400 complex (TIP60-C) is a 20-subunit assembly that impacts chromatin structure via two ...Chromatin structure is a key regulator of DNA transcription, replication, and repair. In humans, the TIP60/EP400 complex (TIP60-C) is a 20-subunit assembly that impacts chromatin structure via two enzymatic activities: ATP-dependent exchange of histone H2A/H2B for H2A.Z/H2B and histone acetylation, which in yeast are carried out by two independent complexes, SWR1 and NuA4, respectively. How these activities are merged in humans into one super-complex and what this association entails for their structure, mechanism and recruitment to chromatin is unknown. Here we describe the 2.4-3.3 Å resolution structure of the endogenous human TIP60-C. We find a three lobed architecture composed of SWR1-like (SWR1L) and NuA4-like (NuA4L) parts, that associate with a TRRAP activator-binding module. The huge EP400 subunit harbors the ATPase motor, traverses twice the junction between SWR1L and NuA4L, and constitutes the scaffold of the three-lobed architecture. NuA4L is completely re-arranged compared to its yeast counterpart. TRRAP is flexibly tethered to NuA4L, in stark contrast to its robust connection to the complete opposite side of yeast NuA4. A modeled nucleosome bound to SWR1L, supported by activity tests, suggests that some aspects of the histone exchange mechanism diverge from the yeast example. Furthermore, a fixed actin module, as opposed to the mobile actin subcomplex in SWR1, the flexibility of TRRAP and the weak effect of extra-nucleosomal DNA on exchange activity, lead to a different, activator-based, mode of enlisting TIP60-C to chromatin.
External links	Nature / PubMed:39260417
Methods	EM (single particle)
Resolution	2.4 - 6.2 Å
Structure data	EMDB-18581: Human Tip60 complex Method: EM (single particle) / Resolution: 2.52 Å EMDB-18591: Human Tip60 complex locally refined on RUVBL1/2 Method: EM (single particle) / Resolution: 2.43 Å EMDB-18597: Human Tip60 complex locally refined on ACTIN and the ATPase domain of EP400 Method: EM (single particle) / Resolution: 5.8 Å EMDB-18598: Tip60 complex locally refined on ARP domain Method: EM (single particle) / Resolution: 2.48 Å 18611 8qr1 EMDB-18611, PDB-8qr1: Cryo-EM structure of the human Tip60 complex Method: EM (single particle) / Resolution: 2.4 Å EMDB-18612: Structure of TRRAP and EP400 in the human Tip 60 complex Method: EM (single particle) / Resolution: 3.52 Å EMDB-18613: TRRAP in human Tip60 complex locally refined 1 Method: EM (single particle) / Resolution: 3.37 Å EMDB-18618: TRRAP in human Tip60 complex locally refined 2 Method: EM (single particle) / Resolution: 4.32 Å 18619 8qri EMDB-18619: TRRAP and EP400 in the human Tip60 complex - composite map PDB-8qri: TRRAP and EP400 in the human Tip60 complex Method: EM (single particle) / Resolution: 3.5 Å EMDB-18794: Human Tip60 complex with bound H2A.Z/H2B Method: EM (single particle) / Resolution: 6.2 Å
Source	homo sapiens (human)
Keywords	TRANSCRIPTION / Eukaryotic transcription / Histone acetyltransferase / chromatin remodeling / Complex