Structural highlights
Function
Q6AZJ8_XENLA
Evolutionary Conservation
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Publication Abstract from PubMed
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 A 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.
Structure of RCC1 chromatin factor bound to the nucleosome core particle.,Makde RD, England JR, Yennawar HP, Tan S Nature. 2010 Sep 30;467(7315):562-6. Epub 2010 Aug 25. PMID:20739938[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Makde RD, England JR, Yennawar HP, Tan S. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature. 2010 Sep 30;467(7315):562-6. Epub 2010 Aug 25. PMID:20739938 doi:10.1038/nature09321