Ontology highlight
ABSTRACT:
SUBMITTER: Aguilar-Gurrieri C
PROVIDER: S-EPMC4931181 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Aguilar-Gurrieri Carmen C Larabi Amédé A Vinayachandran Vinesh V Patel Nisha A NA Yen Kuangyu K Reja Rohit R Ebong Ima-O IO Schoehn Guy G Robinson Carol V CV Pugh B Franklin BF Panne Daniel D
The EMBO journal 20160525 13
Nap1 is a histone chaperone involved in the nuclear import of H2A-H2B and nucleosome assembly. Here, we report the crystal structure of Nap1 bound to H2A-H2B together with in vitro and in vivo functional studies that elucidate the principles underlying Nap1-mediated H2A-H2B chaperoning and nucleosome assembly. A Nap1 dimer provides an acidic binding surface and asymmetrically engages a single H2A-H2B heterodimer. Oligomerization of the Nap1-H2A-H2B complex results in burial of surfaces required ...[more]