The multiplicity of histone chaperone partners, including histone modifiers, nucleosome remodelers and cell-cycle regulators, is relevant to their coordination with key cellular processes.
Histone chaperones participate in the biogenesis, transportation, and deposition of histones. They contribute to processes impacted by nucleosomes including DNA replication, transcription, and epigenetic inheritance. In this issue, Carraro et al.1 reveal an interconnected chaperone network and a surprising function of histone chaperone DAXX in de novo deposition of H3.3K9me3.
The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability …
In this essay we review recent structural insights into histone-chaperone interactions, explore evidence for the existence of a histone chaperoning ‘pathway’ and reconcile how such histone-chaperone interactions may function thermodynamically to assemble nucleosomes and maintain chromatin homeostasis.
The term “histone chaperone” (HC) has evolved continuously as ongoing studies of these molecules revealed new aspects of their function. Originally thought of as little more than “dumb” histone carriers, HCs are now known to be key players at all stages of histones' existence. Chaperones associate with histones upon their synthesis, escort them into the nucleus, and aid in their ...
The team explored about 25 different histone chaperones and found that all of them contribute to stem cell maintenance but in different ways. Two candidates stood out: CAF-1, a chaperone that works during genome duplication, and SPT6, a chaperone that works when genes are turned on.
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.
Nucleosome assembly is crucial for the maintenance of genome stability and epigenetic information and is aided by histone chaperones. This Review discusses recent insights into the mechanisms and ...
Histone chaperones participate in the biogenesis, transportation and deposition of histones. They contribute to processes impacted by nucleosomes including DNA replication, transcription and epigenetic inheritance. In this issue, Carraro et al. 1 reveal an interconnected chaperone network and a surprising function of histone chaperone DAXX in de novo deposition of H3.3K9me3. The nucleosome ...
Histone chaperones are a structurally diverse class of proteins that bind histones and prevent this uncoordinated binding to DNA [14]. Histone chaperones decrease the rate of the formation of improper histone-DNA complexes so that proper nucleosomal histone-DNA complexes can be formed.
Histone chaperones are a large class of proteins responsible for binding the highly basic histone proteins, shielding them from non-specific interactions, facilitating nuclear import of histones, and finally depositing histones onto DNA to form nucleosomes.
Histone chaperones shield nonspecific interactions between the negatively charged DNA and the positively charged histones, to allow the ordered formation of the nucleosome structure. An additional important requisite of histone chaperones is that they are not a permanent component of the final product, the nucleosome.
How one modification can facilitate numerous outcomes is in part determined by the deposition of H3.3 by its chaperones. Two H3.3 amino acids, A87 and G90 control recruitment of its chaperones, histone regulator A (HIRA) and death domain-associated protein/a-thalassemia/mental retardation syndrome X-linked (DAXX/ATRX) complexes [27, 28].
Histone chaperones control nucleosome density and chromatin structure. In yeast, the H3–H4 chaperone Spt2 controls histone deposition at active genes but its roles in metazoan chromatin ...
The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble ...
The factors including ATP- dependent chromatin remodeling complexes, non-histone chromatin-associated proteins, post-translational modification enzymes, and histones chaperones facilitate nucleosome assembly and disassembly by histone transport, deposition, eviction, and storage.
Whether distinct histone chaperone pathways control cell fate and whether they function using related mechanisms remain unclear. To address this, we performed a screen to assess the requirement of diverse histone chaperones in the self-renewal of hematopoietic stem and progenitor cells.
