Divalent Metal- and High Mobility Group N Protein-Dependent Nucleosome Stability and Conformation
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چکیده
منابع مشابه
Divalent Metal- and High Mobility Group N Protein-Dependent Nucleosome Stability and Conformation
High mobility group N proteins (HMGNs) bind specifically to the nucleosome core and act as chromatin unfolding and activating factors. Using an all-Xenopus system, we found that HMGN1 and HMGN2 binding to nucleosomes results in distinct ion-dependent conformation and stability. HMGN2 association with nucleosome core particle or nucleosomal array in the presence of divalent metal triggers a reve...
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Sequence-specific binding of divalent cations to nucleosomal DNA can potentially influence nucleosome position and mobility, as well as modulate interactions with nuclear factors. We define the bonding and specificity of divalent cation interaction with nucleosomal DNA by characterizing Mn2+ binding in the x-ray structure of the nucleosome core particle at 1.9-A resolution. Manganese ions are f...
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15 صفحه اولHigh-mobility group nucleosome-binding protein 1 acts as an alarmin and is critical for lipopolysaccharide-induced immune responses
Alarmins are endogenous mediators capable of promoting the recruitment and activation of antigen-presenting cells (APCs), including dendritic cells (DCs), that can potentially alert host defense against danger signals. However, the relevance of alarmins to the induction of adaptive immune responses remains to be demonstrated. In this study, we report the identification of HMGN1 (high-mobility g...
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ژورنال
عنوان ژورنال: Journal of Nucleic Acids
سال: 2010
ISSN: 2090-021X
DOI: 10.4061/2010/143890