title: CENPs and Sweet Nucleosomes Face the FACT.
abstract: Chaperones mediate vital interactions between histones and DNA during chromatin assembly and reorganization. Two recent studies reveal novel substrates for the essential and conserved histone chaperone FAcilitates Chromatin Transcription (FACT). Prendergast et al. show that FACT helps deposit important histone-fold proteins on centromeres. Raj et al. find that FACT preferentially binds O-GlcNAcylated nucleosomes, suggesting that FACT may contribute to nutrient-regulated cellular programs.
authors: Biomedical Center, Physiological Chemistry, LMU Munich, Großhaderner Street 9, 82152 Planegg-Martinsried, Germany.
authors: Magdalena
authors: M
authors: Murawska
authors: Biomedical Center, Physiological Chemistry, LMU Munich, Großhaderner Street 9, 82152 Planegg-Martinsried, Germany; Center for Integrated Protein Science Munich (CIPSM), 81377 Munich, Germany; Munich Cluster for Systems Neurology (SyNergy), 80336 Munich, Germany. Electronic address: andreas.ladurner@med.lmu.de.
authors: Andreas G
authors: AG
authors: Ladurner
mesh_terms: D002503:Centromere / Q000378:metabolism; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006609:High Mobility Group Proteins / Q000378:metabolism*; D006657:Histones / Q000378:metabolism; D006801:Humans; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism*; D035602:Transcriptional Elongation Factors / Q000378:metabolism*
chemical_list: D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes; C073537:SSRP1 protein, human; D035602:Transcriptional Elongation Factors
keywords: FACT; GlcNAcylation.; histone fold; kinetochore