Results 81 to 90 of about 421 (119)
The ATRX-DAXX histone chaperone complex incorporates H3.3 in heterochromatin in a replication-independent manner. Here, the authors present a high-resolution x-ray crystal structure of an interaction surface between ATRX and DAXX, and characterize ATRX ...
Dominik Hoelper +4 more
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Regulation of histone acetylation and turnover by histone chaperones
Acetylation of histone H3 on lysine 56 occurs on newly synthesized histones in fungal species, and the absence of this modification is associated with extreme sensitivity to genotoxic agents. H3‐K56 acetylation is catalyzed when Rtt109, a distant homolog of p300/CBP acetyltransferases, is stimulated by either ...
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Tipping the balance in histone supply puts genome stability at stake
Specific localization of the histone H3 variant CENP-A at centromeres is key for faithful chromosome segregation during cell division, with CENP-A mislocalization being associated with chromosomal instability and cancer.
Charlène Renaud-Pageot +1 more
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Identification and Characterization of HIRIP3 as a Histone H2A Chaperone
HIRIP3 is a mammalian protein homologous to the yeast H2A.Z deposition chaperone Chz1. However, the structural basis underlying Chz’s binding preference for H2A.Z over H2A, as well as the mechanism through which Chz1 modulates histone deposition or ...
Maria Ignatyeva +8 more
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Histone chaperones and nucleosome assembly
Current Opinion in Structural Biology, 2003Recent structures of the nucleosome core particle reveal details of histone-histone and histone-DNA interactions. These structures have now set the stage for understanding chromatin assembly and dynamics during replication and transcription. Histone chaperones and chromatin remodeling complexes are important in both of these processes.
Christopher W, Akey, Karolin, Luger
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Chaperoning the histone H3 family
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2012Chromatin is a highly dynamic nucleoprotein structure, which orchestrates all nuclear process from DNA replication to DNA repair, fromtranscription to recombination. The proper in vivo assembly of nucleosome, the basic repeating unit of chromatin, requires the deposition of two H3-H4 dimer pairs followed by the addition of two dimers of H2A and H2B ...
Ali, Hamiche, Muhammad, Shuaib
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H3–H4 Histone Chaperone Pathways
Annual Review of Genetics, 2018Nucleosomes compact and organize genetic material on a structural level. However, they also alter local chromatin accessibility through changes in their position, through the incorporation of histone variants, and through a vast array of histone posttranslational modifications.
Prerna, Grover +2 more
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Histone Chaperones: Assisting Histone Traffic and Nucleosome Dynamics
Annual Review of Biochemistry, 2014The functional organization of eukaryotic DNA into chromatin uses histones as components of its building block, the nucleosome. Histone chaperones, which are proteins that escort histones throughout their cellular life, are key actors in all facets of histone metabolism; they regulate the supply and dynamics of histones at chromatin for its assembly ...
Zachary A. Gurard-Levin +2 more
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Histone chaperones: an escort network regulating histone traffic
Nature Structural & Molecular Biology, 2007In eukaryotes, DNA is organized into chromatin in a dynamic manner that enables it to be accessed for processes such as transcription and repair. Histones, the chief protein component of chromatin, must be assembled, replaced or exchanged to preserve or change this organization according to cellular needs.
Leanne, De Koning +3 more
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Structure and function of histone chaperone FACT
Molecular Biology, 2015FACT is heterodimer protein complex and histone chaperone that plays an important role in maintaining and modifying chromatin structure during various DNA-dependent processes. FACT is involved in nucleosome assembly de novo and in the preservation and recovery of the nucleosome structure during and after transcription, replication and repair of DNA ...
M T, Bondarenko +6 more
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