Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Nature September 30, 2010; 467 (7315): 562-6.

Structure of RCC1 chromatin factor bound to the nucleosome core particle.

Makde RD , England JR , Yennawar HP , Tan S .

The small GTPase Ran enzyme regulates critical eukaryotic cellular functions including nuclear transport and mitosis through the creation of a RanGTP gradient around the chromosomes. This concentration gradient is created by the chromatin-bound RCC1 (regulator of chromosome condensation) protein, which recruits Ran to nucleosomes and activates Ran''s nucleotide exchange activity. Although RCC1 has been shown to bind directly with the nucleosome, the molecular details of this interaction were not known. Here we determine the crystal structure of a complex of Drosophila RCC1 and the nucleosome core particle at 2.9 Å resolution, providing an atomic view of how a chromatin protein interacts with the histone and DNA components of the nucleosome. Our structure also suggests that the Widom 601 DNA positioning sequence present in the nucleosomes forms a 145-base-pair nucleosome core particle, not the expected canonical 147-base-pair particle.

PubMed ID: 20739938
PMC ID: PMC3168546
Article link: Nature
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: h2ac21 h2bc21 h4c4 ran rcc1 tbx2

Article Images: [+] show captions
References [+] :
Adams, PHENIX: building new software for automated crystallographic structure determination. 2002, Pubmed