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 the 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 affects chromatin structure through 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 affects chromatin structure through two enzymatic activities: ATP-dependent exchange of histone H2A-H2B for H2A.Z-H2B, and histone acetylation. In yeast, however, these activities are performed by two independent complexes-SWR1 and NuA4, respectively. How the activities of the two complexes are merged into one supercomplex in humans, and what this association entails for the structure and mechanism of the proteins and their recruitment to chromatin, are unknown. Here we describe the structure of the endogenous human TIP60-C. We find a three-lobed architecture composed of SWR1-like (SWR1L) and NuA4-like (NuA4L) parts, which associate with a TRRAP activator-binding module. The huge EP400 subunit contains the ATPase motor, traverses the junction between SWR1L and NuA4L twice and constitutes the scaffold of the three-lobed architecture. NuA4L is completely rearranged compared with its yeast counterpart. TRRAP is flexibly tethered to NuA4L-in stark contrast to its robust connection to the completely opposite side of NuA4 in yeast. A modelled nucleosome bound to SWR1L, supported by tests of TIP60-C activity, suggests that some aspects of the histone exchange mechanism diverge from what is seen in yeast. Furthermore, a fixed actin module (as opposed to the mobile actin subcomplex in SWR1; ref. ), the flexibility of TRRAP and the weak effect of extranucleosomal 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