منابع مشابه
Chz1, a nuclear chaperone for histone H2AZ.
The histone variant H2AZ marks nucleosomes flanking the promoters of most genes of budding yeast. The incorporation of H2AZ into chromatin is dependent on the SWR1 complex, which catalyses the replacement of conventional histone H2A with H2AZ. In cells, the pool of unincorporated histone H2AZ has previously been found in association with Nap1, a chaperone for conventional histone H2A-H2B. Here,...
متن کاملImportance of Electrostatic Interactions in the Association of Intrinsically Disordered Histone Chaperone Chz1 and Histone H2A.Z-H2B
Histone chaperones facilitate assembly and disassembly of nucleosomes. Understanding the process of how histone chaperones associate and dissociate from the histones can help clarify their roles in chromosome metabolism. Some histone chaperones are intrinsically disordered proteins (IDPs). Recent studies of IDPs revealed that the recognition of the biomolecules is realized by the flexibility an...
متن کاملPreferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling.
The yeast histone variant H2AZ (Htz1) is implicated in transcription activation, prevention of the ectopic spread of heterochromatin, and genome integrity. Our genome-wide localization analysis revealed that Htz1 is widely, but nonrandomly, distributed throughout the genome in an SWR1-dependent manner. We found that Htz1 is enriched in intergenic regions compared with coding regions. Its occupa...
متن کاملHistone chaperone regulates replication
F orm follows physics in the fl y eye, say The idea that a small set of physical forces governs the shape of tissues goes back at least a hundred years, but there has been little evidence to support it. Now, Hilgenfeldt et al. show that just two parameters— cell elasticity and adhesion strength—can account for the arrangement of cells in the ommatidium, the 20-cell subunit of the fl y's compoun...
متن کاملHistone acetylation-independent transcription stimulation by a histone chaperone
Histone chaperones are thought to be important for maintaining the physiological activity of histones; however, their exact roles are not fully understood. The physiological function of template activating factor (TAF)-I, one of the histone chaperones, also remains unclear; however, its biochemical properties have been well studied. By performing microarray analyses, we found that TAF-I stimula...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 2007
ISSN: 1097-2765
DOI: 10.1016/j.molcel.2006.12.015