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Structure of RCC1 chromatin factor bound to the nucleosome core particle

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  • Ravindra D. Makde

    (Center for Eukaryotic Gene Regulation, The Pennsylvania State University
    Present addresses: High Pressure and Synchrotron Radiation Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India (R.D.M.); Temple University School of Medicine, 3500 North Broad Street, Philadelphia, Pennsylvania 19140, USA (J.R.E.).)

  • Joseph R. England

    (Center for Eukaryotic Gene Regulation, The Pennsylvania State University
    Present addresses: High Pressure and Synchrotron Radiation Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India (R.D.M.); Temple University School of Medicine, 3500 North Broad Street, Philadelphia, Pennsylvania 19140, USA (J.R.E.).)

  • Hemant P. Yennawar

    (Center for Eukaryotic Gene Regulation, The Pennsylvania State University)

  • Song Tan

    (Center for Eukaryotic Gene Regulation, The Pennsylvania State University)

Abstract

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.

Suggested Citation

  • Ravindra D. Makde & Joseph R. England & Hemant P. Yennawar & Song Tan, 2010. "Structure of RCC1 chromatin factor bound to the nucleosome core particle," Nature, Nature, vol. 467(7315), pages 562-566, September.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7315:d:10.1038_nature09321
    DOI: 10.1038/nature09321
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    Cited by:

    1. Harsh Nagpal & Ahmad Ali-Ahmad & Yasuhiro Hirano & Wei Cai & Mario Halic & Tatsuo Fukagawa & Nikolina Sekulić & Beat Fierz, 2023. "CENP-A and CENP-B collaborate to create an open centromeric chromatin state," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Vivekanandan Ramalingam & Xinyang Yu & Brian D. Slaughter & Jay R. Unruh & Kaelan J. Brennan & Anastasiia Onyshchenko & Jeffrey J. Lange & Malini Natarajan & Michael Buck & Julia Zeitlinger, 2023. "Lola-I is a promoter pioneer factor that establishes de novo Pol II pausing during development," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Ai Kiyomitsu & Toshiya Nishimura & Shiang Jyi Hwang & Satoshi Ansai & Masato T. Kanemaki & Minoru Tanaka & Tomomi Kiyomitsu, 2024. "Ran-GTP assembles a specialized spindle structure for accurate chromosome segregation in medaka early embryos," Nature Communications, Nature, vol. 15(1), pages 1-19, December.

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