Structure of the human TIP60-C histone exchange and acetyltransferase complex.

ABSTRACT: Chromatin structure is a key regulator of DNA transcription, replication and repair¹. 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^2,3. 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 (NuA

SUBMITTER: Li C 

PROVIDER: S-EPMC11578891 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature