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      The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization.

      The Journal of Biological Chemistry

      Animals, Chromatin Assembly and Disassembly, physiology, DNA Repair, DNA Replication, DNA-Binding Proteins, metabolism, High Mobility Group Proteins, Histones, Humans, Models, Biological, Molecular Chaperones, Nucleosomes, Structure-Activity Relationship, Transcription, Genetic, Transcriptional Elongation Factors

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          Abstract

          Changes in chromatin architecture induced by epigenetic mechanisms are essential for normal cellular processes such as gene expression, DNA repair, and cellular division. Compact chromatin presents a barrier to these processes and is highly regulated by epigenetic markers binding to components of the nucleosome. Histone modifications directly influence chromatin dynamics and facilitate recruitment of additional factors such as chromatin remodelers and histone chaperones. One member of this last class of factors, FACT (facilitates chromatin transcription), is categorized as a histone chaperone critical for nucleosome reorganization during replication, transcription, and DNA repair. Significant discoveries regarding the role of histone chaperones and specifically FACT have come over the past dozen years from a number of independent laboratories. Here, we review the structural and biophysical basis for FACT-mediated nucleosome reorganization and discuss up-to-date models for FACT function.

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          Author and article information

          Journal
          21454601
          3099653
          10.1074/jbc.R110.180778

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