Results 231 to 240 of about 17,972 (261)

DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network [PDF]

open access: yesMolecular Cell, 2021
From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear.
Colin M Hammond   +2 more
exaly   +8 more sources
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Histone chaperone networks shaping chromatin function

open access: yesNature Reviews Molecular Cell Biology, 2017
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
Colin M Hammond   +2 more
exaly   +2 more sources

Histone Chaperones: Assisting Histone Traffic and Nucleosome Dynamics

Annual Review of Biochemistry, 2014
The 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
exaly   +3 more sources

Histone chaperones, a supporting role in the limelight

Biochimica Et Biophysica Acta Gene Regulatory Mechanisms, 2004
In eukaryotic cells, highly basic histone proteins are associated with the DNA to form the nucleosome, the fundamental unit of chromatin. Histones are closely escorted by histone chaperones from their point of synthesis up to their delivery site. We will present an overview of the histone chaperones identified to date with their various roles, in an ...
Alejandra Loyola, Genevieve Almouzni
exaly   +3 more sources

Histone chaperones and nucleosome assembly

Current Opinion in Structural Biology, 2003
Recent 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
openaire   +2 more sources

Histone chaperones link histone nuclear import and chromatin assembly [PDF]

open access: yesBiochimica Et Biophysica Acta - Gene Regulatory Mechanisms, 2012
Histone chaperones are proteins that shield histones from nonspecific interactions until they are assembled into chromatin. After their synthesis in the cytoplasm, histones are bound by different histone chaperones, subjected to a series of posttranslational modifications and imported into the nucleus.
Lucy F Pemberton
exaly   +4 more sources

Histone chaperones: an escort network regulating histone traffic

Nature Structural & Molecular Biology, 2007
In 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
openaire   +2 more sources

Structure and function of histone chaperone FACT

Molecular Biology, 2015
FACT 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
openaire   +2 more sources

H3–H4 Histone Chaperone Pathways

Annual Review of Genetics, 2018
Nucleosomes 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
openaire   +2 more sources

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