Structure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone FACT
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Title
Structure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone FACT
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 15, Pages 10188-10194
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2013-02-16
DOI
10.1074/jbc.c113.451369
References
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Related references
Note: Only part of the references are listed.- Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106
- (2012) Dan Su et al. NATURE
- Identification of Mutant Versions of the Spt16 Histone Chaperone That Are Defective for Transcription-Coupled Nucleosome Occupancy in Saccharomyces cerevisiae
- (2012) Sarah J. Hainer et al. G3-Genes Genomes Genetics
- The role of FACT in making and breaking nucleosomes
- (2011) Tim Formosa Biochimica et Biophysica Acta-Gene Regulatory Mechanisms
- Insight Into the Mechanism of Nucleosome Reorganization From Histone Mutants That Suppress Defects in the FACT Histone Chaperone
- (2011) Laura McCullough et al. GENETICS
- The Histone Chaperone FACT: Structural Insights and Mechanisms for Nucleosome Reorganization
- (2011) Duane D. Winkler et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Histone Chaperone FACT Coordinates Nucleosome Interaction through Multiple Synergistic Binding Events
- (2011) Duane D. Winkler et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mutant Versions of the S. cerevisiae Transcription Elongation Factor Spt16 Define Regions of Spt16 That Functionally Interact with Histone H3
- (2011) Catherine N. Myers et al. PLoS One
- Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing
- (2011) R. M. Zunder et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Structural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing
- (2009) Yiwei Liu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Histone Chaperone Spt16 Promotes Redeposition of the Original H3-H4 Histones Evicted by Elongating RNA Polymerase
- (2009) Adil Jamai et al. MOLECULAR CELL
- yFACT Induces Global Accessibility of Nucleosomal DNA without H2A-H2B Displacement
- (2009) Hua Xin et al. MOLECULAR CELL
- The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module
- (2008) Tobias Stuwe et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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