1 research outputs found
Structural and functional characterisation of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.
Recent proteomic studies have identified a novel histone deacetylase complex that is
upregulated during mitosis and is associated with cyclin A. This complex is conserved
from nematodes to man and contains histone deacetylases 1 and 2, the MIDEAS
corepressor protein and a protein called DNTTIP1 whose function was hitherto poorly
understood. Here we report the structures of two domains from DNTTIP1. The aminoterminal
region forms a tight dimerisation domain with a novel structural fold that
interacts with and mediates assembly of the HDAC1:MIDEAS complex. The carboxyterminal
domain of DNTTIP1 has a structure related to the SKI/SNO/DAC domain,
despite lacking obvious sequence homology. We show that this domain in DNTTIP1
mediates interaction with both DNA and nucleosomes. Thus DNTTIP1 acts as a dimeric
chromatin binding module in the HDAC1:MIDEAS corepressor complex