IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v389y1997i6648d10.1038_38444.html
   My bibliography  Save this article

Crystal structure of the nucleosome core particle at 2.8 Å resolution

Author

Listed:
  • Karolin Luger

    (Institut für Molekularbiologie und Biophysik ETHZ)

  • Armin W. Mäder

    (Institut für Molekularbiologie und Biophysik ETHZ)

  • Robin K. Richmond

    (Institut für Molekularbiologie und Biophysik ETHZ)

  • David F. Sargent

    (Institut für Molekularbiologie und Biophysik ETHZ)

  • Timothy J. Richmond

    (Institut für Molekularbiologie und Biophysik ETHZ)

Abstract

The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it. Both histone/histone and histone/DNA interactions depend on the histone fold domains and additional, well ordered structure elements extending from this motif. Histone amino-terminal tails pass over and between the gyres of the DNA superhelix to contact neighbouring particles. The lack of uniformity between multiple histone/DNA-binding sites causes the DNA to deviate from ideal superhelix geometry.

Suggested Citation

  • Karolin Luger & Armin W. Mäder & Robin K. Richmond & David F. Sargent & Timothy J. Richmond, 1997. "Crystal structure of the nucleosome core particle at 2.8 Å resolution," Nature, Nature, vol. 389(6648), pages 251-260, September.
    • Handle: RePEc:nat:nature:v:389:y:1997:i:6648:d:10.1038_38444
    DOI: 10.1038/38444
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/38444
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/38444?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Namrata Kumar & Arjan F. Theil & Vera Roginskaya & Yasmin Ali & Michael Calderon & Simon C. Watkins & Ryan P. Barnes & Patricia L. Opresko & Alex Pines & Hannes Lans & Wim Vermeulen & Bennett Houten, 2022. "Global and transcription-coupled repair of 8-oxoG is initiated by nucleotide excision repair proteins," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Nithya Ramakrishnan & Sibi Raj B Pillai & Ranjith Padinhateeri, 2022. "High fidelity epigenetic inheritance: Information theoretic model predicts threshold filling of histone modifications post replication," PLOS Computational Biology, Public Library of Science, vol. 18(2), pages 1-22, February.
    3. Marko Dunjić & Felix Jonas & Gilad Yaakov & Roye More & Yoav Mayshar & Yoach Rais & Ayelet-Hashahar Orenbuch & Saifeng Cheng & Naama Barkai & Yonatan Stelzer, 2023. "Histone exchange sensors reveal variant specific dynamics in mouse embryonic stem cells," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    4. Tyler M. Weaver & Nicole M. Hoitsma & Jonah J. Spencer & Lokesh Gakhar & Nicholas J. Schnicker & Bret D. Freudenthal, 2022. "Structural basis for APE1 processing DNA damage in the nucleosome," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    5. Victoria S. Frisbie & Hideharu Hashimoto & Yixuan Xie & Francisca N. De Luna Vitorino & Josue Baeza & Tam Nguyen & Zhangerjiao Yuan & Janna Kiselar & Benjamin A. Garcia & Erik W. Debler, 2024. "Two DOT1 enzymes cooperatively mediate efficient ubiquitin-independent histone H3 lysine 76 tri-methylation in kinetoplastids," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    6. Jiayi Fan & Andrew T. Moreno & Alexander S. Baier & Joseph J. Loparo & Craig L. Peterson, 2022. "H2A.Z deposition by SWR1C involves multiple ATP-dependent steps," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    7. Yu Zhang & Min Ma & Meng Liu & Aiqing Sun & Xiaoyun Zheng & Kunpeng Liu & Chunmei Yin & Chuanshun Li & Cizhong Jiang & Xiaoyu Tu & Yuda Fang, 2023. "Histone H2A monoubiquitination marks are targeted to specific sites by cohesin subunits in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    8. Shuxiang Li & Tiejun Wei & Anna R. Panchenko, 2023. "Histone variant H2A.Z modulates nucleosome dynamics to promote DNA accessibility," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    9. Masaki Kikuchi & Satoshi Morita & Masatoshi Wakamori & Shin Sato & Tomomi Uchikubo-Kamo & Takehiro Suzuki & Naoshi Dohmae & Mikako Shirouzu & Takashi Umehara, 2023. "Epigenetic mechanisms to propagate histone acetylation by p300/CBP," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    10. Timothy A. Daugird & Yu Shi & Katie L. Holland & Hosein Rostamian & Zhe Liu & Luke D. Lavis & Joseph Rodriguez & Brian D. Strahl & Wesley R. Legant, 2024. "Correlative single molecule lattice light sheet imaging reveals the dynamic relationship between nucleosomes and the local chromatin environment," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    11. Anfeng Luo & Jingwei Kong & Jun Chen & Xue Xiao & Jie Lan & Xiaorong Li & Cuifang Liu & Peng-Ye Wang & Guohong Li & Wei Li & Ping Chen, 2023. "H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    12. Dian Spakman & Tinka V. M. Clement & Andreas S. Biebricher & Graeme A. King & Manika I. Singh & Ian D. Hickson & Erwin J. G. Peterman & Gijs J. L. Wuite, 2022. "PICH acts as a force-dependent nucleosome remodeler," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    13. Jaeyoon Lee & Meiling Wu & James T. Inman & Gundeep Singh & Seong ha Park & Joyce H. Lee & Robert M. Fulbright & Yifeng Hong & Joshua Jeong & James M. Berger & Michelle D. Wang, 2023. "Chromatinization modulates topoisomerase II processivity," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    14. Rina Hirano & Haruhiko Ehara & Tomoya Kujirai & Tamami Uejima & Yoshimasa Takizawa & Shun-ichi Sekine & Hitoshi Kurumizaka, 2022. "Structural basis of RNA polymerase II transcription on the chromatosome containing linker histone H1," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    15. Xiaowei Xu & Shoufu Duan & Xu Hua & Zhiming Li & Richard He & Zhiguo Zhang, 2022. "Stable inheritance of H3.3-containing nucleosomes during mitotic cell divisions," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    16. Un Seng Chio & Eugene Palovcak & Anton A. A. Smith & Henriette Autzen & Elise N. Muñoz & Zanlin Yu & Feng Wang & David A. Agard & Jean-Paul Armache & Geeta J. Narlikar & Yifan Cheng, 2024. "Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    17. Allison Ballandras-Colas & Vidya Chivukula & Dominika T. Gruszka & Zelin Shan & Parmit K. Singh & Valerie E. Pye & Rebecca K. McLean & Gregory J. Bedwell & Wen Li & Andrea Nans & Nicola J. Cook & Hind, 2022. "Multivalent interactions essential for lentiviral integrase function," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    18. Zhen Hou & Frank Nightingale & Yanan Zhu & Craig MacGregor-Chatwin & Peijun Zhang, 2023. "Structure of native chromatin fibres revealed by Cryo-ET in situ," Nature Communications, Nature, vol. 14(1), pages 1-7, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:389:y:1997:i:6648:d:10.1038_38444. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.