Tsunaka, Y., Fujiwara, Y., Oyama, T., Hirose, S. Describes the histone chaperone function of the FACT complex and its ability to promote H2A–H2B eviction and transcription through chromatin. FACT facilitates transcription-dependent nucleosome alteration. Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. Also provides the first structure of a co-chaperone complex, the MCM2–H3–H4–ASF1 complex. Provides the crystal structure of MCM2 with a H3–H4 tetramer and shows that MCM2 in vivo chaperones H3–H4 alone and as part of the replicative helicase. A unique binding mode enables MCM2 to chaperone histones H3–H4 at replication forks. Presents the structure of human SPT2 bound to a H3–H4 tetramer and shows that histone-binding mutants of Spt2 in yeast phenocopy Spt2 deletion in failing to suppress cryptic transcription. Structure–function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2. Structure of the variant histone H3.3–H4 heterodimer in complex with its chaperone DAXX. This study uses a novel approach to reconstitute the histone chaperone complex from unfolded components. Defines the structural specificity of DAXX for H3.3–H4 and describes the sequestration of the H3 α N helix and H4 C terminus in non-nucleosomal conformations. DAXX envelops a histone H3.3–H4 dimer for H3.3-specific recognition. Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats. Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones. AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation. Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response. Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation. References 22 and 23 provide the first co-crystal structure of a histone chaperone in complex with its histone cargo, providing a molecular description of how Asf1 chaperones an H3–H4 dimer. Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4. Structural basis for the histone chaperone activity of Asf1. Structure and function of the conserved core of histone deposition protein Asf1. Thermodynamic model for Nap1–histone Interactions. Thermodynamic study detailing the role of Nap1 in nucleosome assembly, showing how histone chaperones can buffer interactions between histones and DNA.Īndrews, A. The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions. The right place at the right time: chaperoning core histone variants. Shows that the checkpoint kinase Rad53 monitors the level of soluble histones and that accumulation of excess histones caused by mutation of Rad53 jeopardizes genome stability. Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission. New histone supply regulates replication fork speed and PCNA unloading. The histone chaperone CAF-1 safeguards somatic cell identity. Early embryonic-like cells are induced by downregulating replication-dependent chromatin assembly. Mislocalization of the centromeric histone variant CenH3/CENP-A in human cells depends on the chaperone DAXX. Mislocalization of the Drosophila centromere-specific histone CID promotes formation of functional ectopic kinetochores. A network of players in H3 histone variant deposition and maintenance at centromeres. Rapid induction of alternative lengthening of telomeres by depletion of the histone chaperone ASF1. Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail. Histone chaperones: assisting histone traffic and nucleosome dynamics. Assembling chromatin: the long and winding road. Chromatin plasticity in response to DNA damage: the shape of things to come. Chromatin replication and epigenome maintenance. Histone exchange, chromatin structure and the regulation of transcription. The first description of histone chaperone function elucidated by classical biochemical approaches probing the physicochemical nature of the association between nucleoplasmin and histones. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA.
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