Results 21 to 30 of about 56,937 (264)

Histone chaperones in nucleosome eviction and histone exchange [PDF]

open access: yesCurrent 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

Mitochondrial stress in advanced fibrosis and cirrhosis associated with chronic hepatitis B, chronic hepatitis C, or nonalcoholic steatohepatitis

open access: yesHepatology, EarlyView., 2022
Adaptive mitochondrial mechanisms allow mitochondrial resilience and prevent the worsening of fibrosis, while deregulation of these mechanisms promotes the progression from no/minimal‐mild (F0‐F2) fibrosis to advanced fibrosis and cirrhosis (F3‐F4). Abstract Background and Aims Hepatitis B virus (HBV) infection causes oxidative stress (OS) and alters ...
Dimitri Loureiro   +17 more
wiley   +1 more source

The histone chaperone ANP32B regulates chromatin incorporation of the atypical human histone variant macroH2A

open access: yesCell Reports, 2023
Summary: All vertebrate genomes encode for three large histone H2A variants that have an additional metabolite-binding globular macrodomain module, macroH2A. MacroH2A variants impact heterochromatin organization and transcription regulation and establish
Imke K. Mandemaker   +9 more
doaj   +1 more source

HIRA, a DiGeorge Syndrome Candidate Gene, Confers Proper Chromatin Accessibility on HSCs and Supports All Stages of Hematopoiesis

open access: yesCell Reports, 2020
Summary: HIRA is a histone chaperone that deposits the histone variant H3.3 in transcriptionally active genes. In DiGeorge syndromes, a DNA stretch encompassing HIRA is deleted.
Chao Chen   +9 more
doaj   +1 more source

ATAD2 controls chromatin-bound HIRA turnover

open access: yesLife Science Alliance, 2021
Parallel study of multiple model systems points to the evolutionary conserved protein ATAD2, as a critical histone chaperone auxiliary factor. Taking advantage of the evolutionary conserved nature of ATAD2, we report here a series of parallel functional ...
Tao Wang   +17 more
doaj   +1 more source

Towards a mechanism for histone chaperones [PDF]

open access: yesBiochimica 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

open access: yesCroatica 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

Dissecting regulatory pathways for transcription recovery following DNA damage reveals a non-canonical function of the histone chaperone HIRA

open access: yesNature 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

The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution [PDF]

open access: yes, 2013
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a ...
Andrew Bowman   +53 more
core   +8 more sources

Histone chaperone specificity in Rtt109 activation [PDF]

open access: yesNature 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

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