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Research Article
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The histone chaperone FACT modulates nucleosome structure by tethering its components

View ORCID ProfileTao Wang, Yang Liu, Garrett Edwards, Daniel Krzizike, Hataichanok Scherman, View ORCID ProfileKarolin Luger  Correspondence email
Tao Wang
1Department of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO, USA
2Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA
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  • ORCID record for Tao Wang
Yang Liu
1Department of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO, USA
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Garrett Edwards
1Department of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO, USA
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Daniel Krzizike
1Department of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO, USA
2Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA
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Hataichanok Scherman
2Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA
3Institute for Genome Architecture and Function, Colorado State University, Fort Collins, CO, USA
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Karolin Luger
1Department of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO, USA
3Institute for Genome Architecture and Function, Colorado State University, Fort Collins, CO, USA
4Howard Hughes Medical Institute, Chevy Chase, MD, USA
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  • ORCID record for Karolin Luger
  • For correspondence: karolin.luger{at}colorado.edu
Published 10 July 2018. DOI: 10.26508/lsa.201800107
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Article Information

vol. 1 no. 4 e201800107
DOI 
https://doi.org/10.26508/lsa.201800107
PubMed 
30456370

Published By 
Life Science Alliance
Online ISSN 
2575-1077
History 
  • Received June 14, 2018
  • Revision received June 29, 2018
  • Accepted June 29, 2018
  • Published online July 10, 2018.

Copyright & Usage 
© 2018 Wang et al. This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).

Author Information

  1. Tao Wang1,2,*,
  2. Yang Liu1,*,
  3. Garrett Edwards1,
  4. Daniel Krzizike1,2,
  5. Hataichanok Scherman2,3 and
  6. Karolin Luger1,3,4⇑
  1. 1Department of Chemistry and Biochemistry, University of Colorado Boulder, Boulder, CO, USA
  2. 2Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA
  3. 3Institute for Genome Architecture and Function, Colorado State University, Fort Collins, CO, USA
  4. 4Howard Hughes Medical Institute, Chevy Chase, MD, USA
  1. Correspondence: karolin.luger{at}colorado.edu
  1. ↵* Tao Wang and Yang Liu contributed equally to this work.

View Full Text

Funding

  • Howard Hughes Medical Institute

    NIH-GM-067777
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FACT interactions with partial nucleosomes
Tao Wang, Yang Liu, Garrett Edwards, Daniel Krzizike, Hataichanok Scherman, Karolin Luger
Life Science Alliance Jul 2018, 1 (4) e201800107; DOI: 10.26508/lsa.201800107

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FACT interactions with partial nucleosomes
Tao Wang, Yang Liu, Garrett Edwards, Daniel Krzizike, Hataichanok Scherman, Karolin Luger
Life Science Alliance Jul 2018, 1 (4) e201800107; DOI: 10.26508/lsa.201800107
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Volume 1, No. 4
August 2018
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  • Chromatin & Epigenetics

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Cited By...

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  • Abo1 ATPase facilitates the dissociation of FACT from chromatin
  • Glutamylation of Npm2 and Nap1 acidic disordered regions increases DNA charge mimicry to enhance chaperone efficiency
  • A FACT-ETS-1 Antiviral Response Pathway Restricts Viral Replication and is Countered by Poxvirus A51R Proteins
  • FACT regulates pluripotency through distal regulation of gene expression in murine embryonic stem cells
  • Assignment of structural transitions during mechanical unwrapping of nucleosomes and their disassembly products
  • Melbournevirus-encoded histone doublets are recruited to virus particles and form destabilized nucleosome-like structures
  • Proteasomal Regulation of Mammalian SPT16 in Controlling Transcription
  • Cockayne syndrome B protein acts as an ATP-dependent processivity factor that helps RNA polymerase II overcome nucleosome barriers
  • FACT is recruited to the +1 nucleosome of transcribed genes and spreads in a Chd1-dependent manner
  • Nucleosome composition regulates the histone H3 tail conformational ensemble and accessibility
  • The histone chaperoning pathway: from ribosome to nucleosome
  • Establishment and Maintenance of Chromatin Architecture Are Promoted Independently of Transcription by the Histone Chaperone FACT and H3-K56 Acetylation in Saccharomyces cerevisiae
  • Mechanism of FACT removal from transcribed genes by anticancer drugs curaxins
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