RT Journal Article
SR Electronic
T1 Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 089581
DO 10.1101/089581
A1 Ramasubramanian Sundaramoorthy
A1 Amanda L. Hughes
A1 Vijender Singh
A1 Nicola Wiechens
A1 Daniel P. Ryan
A1 Hassane El-Mkami
A1 Maxim Petoukhov
A1 Dmitri I. Svergun
A1 Barbara Treutlein
A1 Monika Fischer
A1 Jens Michaelis
A1 Bettina Böttcher
A1 David G. Norman
A1 Tom Owen-Hughes
YR 2016
UL http://biorxiv.org/content/early/2016/11/26/089581.abstract
AB The yeast Chd1 protein acts to position nucleosomes across genomes. Here we model the structure of the Chd1 protein in solution and when bound to nucleosomes. In the apo state the DNA binding domain contacts the edge of the nucleosome while in the presence of the non-hydrolyzable ATP analog, ADP-beryllium fluoride, we observe additional interactions between the ATPase domain and the adjacent DNA gyre 1.5 helical turns from the dyad axis of symmetry. Binding in this conformation involves unravelling the outer turn of nucleosomal DNA and requires substantial reorientation of the DNA binding domain with respect to the ATPase domains. The orientation of the DNA-binding domain is mediated by sequences in the N-terminus and mutations to this part of the protein have positive and negative effects on Chd1 activity. These observations indicate that the unfavourable alignment of C-terminal DNA binding region in solution contributes to an auto-inhibited state.