Results 11 to 20 of about 421 (119)
Histone chaperone-mediated nucleosome assembly process. [PDF]
PLoS ONE, 2015 A huge amount of information is stored in genomic DNA and this stored information resides inside the nucleus with the aid of chromosomal condensation factors.
Hsiu-Fang Fan +4 more
doaj +4 more sources
Histones, histone chaperones and nucleosome assembly [PDF]
Protein & Cell, 2010 Chromatin structure governs a number of cellular processes including DNA replication, transcription, and DNA repair. During DNA replication, chromatin structure including the basic repeating unit of chromatin, the nucleosome, is temporarily disrupted, and then reformed immediately after the passage of the replication fork.
Rebecca J, Burgess, Zhiguo, Zhang
openaire +2 more sources
Histone transfer among chaperones [PDF]
Biochemical Society Transactions, 2012 The eukaryotic processes of nucleosome assembly and disassembly govern chromatin dynamics, in which histones exchange in a highly regulated manner to promote genome accessibility for all DNA-dependent processes. This regulation is partly carried out by histone chaperones, which serve multifaceted roles in co-ordinating the interactions of histone ...
Wallace H, Liu, Mair E A, Churchill
openaire +2 more sources
Histone chaperones regulate histone exchange during transcription [PDF]
The EMBO Journal, 2007 Transcription by RNA polymerase II is accompanied by dynamic changes in chromatin, including the eviction/deposition of nucleosomes or the covalent modification of histone subunits. This study examined the role of the histone H3/H4 chaperones, Asf1 and HIR, in histone mobility during transcription, with particular focus on the histone exchange pathway,
Hye-Jin, Kim +4 more
openaire +2 more sources
Histone chaperones in nucleosome eviction and histone exchange [PDF]
Current Opinion in Structural Biology, 2008 The recent two years have led to the realization that histone chaperones contribute to the delicate balance between nucleosome assembly and re-assembly during transcription, and may in fact be involved as much in histone eviction as they are in chromatin assembly.
Young-Jun, Park, Karolin, Luger
openaire +2 more sources
Towards a mechanism for histone chaperones [PDF]
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2012 Histone chaperones can be broadly defined as histone-binding proteins that influence chromatin dynamics in an ATP-independent manner. Their existence reflects the importance of chromatin homeostasis and the unique and unusual biochemistry of the histone proteins.
Elsässer SJ, D'Arcy S
openaire +3 more sources
Simplified Method for Rapid Purification of Soluble Histones
Croatica Chemica Acta, 2016 Functional and structural studies of histone-chaperone complexes, nucleosome modifications, their interactions with remodelers and regulatory proteins rely on obtaining recombinant histones from bacteria.
Nives Ivić +3 more
doaj +1 more source
Nature Communications, 2021 How gene expression reactivation is promoted following DNA damage is not yet clear. Here, the authors identify a role for the human histone chaperone complex HIRA in transcription restart following UV damage independently of its function in new H3.3 ...
Déborah Bouvier +5 more
doaj +1 more source
Histone Chaperone Nrp1 Mutation Affects the Acetylation of H3K56 in Tetrahymena thermophila
Cells, 2022 Histone modification and nucleosome assembly are mainly regulated by various histone-modifying enzymes and chaperones. The roles of histone-modification enzymes have been well analyzed, but the molecular mechanism of histone chaperones in histone ...
Yinjie Lian +4 more
doaj +1 more source
Histone chaperone specificity in Rtt109 activation [PDF]
Nature Structural & Molecular Biology, 2008 Rtt109 is a histone acetyltransferase that requires a histone chaperone for the acetylation of histone 3 at lysine 56 (H3K56). Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair. Here we show that both Rtt109 and Vps75 bind histones with high affinity, but only the complex is efficient for catalysis.
Young-Jun, Park +4 more
openaire +2 more sources