Histone H2ax Phosphorylation
Histone H2ax Phosphorylation - Related Videos
02:32
Histone Modification
0 Views •
2020
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression. Acetylation The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
01:02
Phosphorylation
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2019
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins. During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
02:30
Histone Variants at the Centromere
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2020
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
09:26
Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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Cited by 1 •
2017
This protocol describes the reconstitution of nucleosomes containing differentially isotope-labeled sister histones. At the same time, asymmetrically post-translationally modified nucleosomes can be generated after using a premodified histone copy. These preparations can be readily used to study modification crosstalk mechanisms, simultaneously on both sister histones, by using high-resolution NMR spectroscopy.
09:47
Analysis of Histone Antibody Specificity with Peptide Microarrays
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Cited by 22 •
2017
This manuscript describes methods for applying peptide microarray technology to specificity profiling of antibodies that recognize histones and their post-translational modifications.
FAQs
ATM, ATR, and DNA-PK provide the kinase activity that responds to a DNA double-strand break by modifying H2AX. Their involvement connects the damage site to a chromatin-based response rather than treating the break as an isolated DNA lesion. Examining this kinase-dependent step helps researchers relate γ-H2AX formation to activation of DNA repair and checkpoint pathways.
After formation near a break, γ-H2AX extends across surrounding chromatin. This spatial expansion creates a larger chromatin region that helps recruit DNA repair and checkpoint proteins. The spreading feature amplifies the local damage signal, allowing the response to involve chromatin around the lesion rather than remaining restricted to the precise site of the DNA break.
γ-H2AX links a DNA double-strand break to checkpoint signaling by creating a chromatin-associated signal that helps recruit checkpoint proteins. This recruitment can coordinate detection of the lesion with the broader response to damage, while the surrounding chromatin signal indicates that the response extends beyond the exact break site. It therefore connects local damage with genome surveillance.
Researchers choose among immunofluorescence, western blotting, and flow cytometry according to the readout needed. Immunofluorescence detects γ-H2AX foci, whereas western blotting and flow cytometry provide other ways to measure the phosphorylation-associated damage response. Applying these complementary approaches can help quantify DNA damage and repair in experimental biology.
By measuring γ-H2AX, researchers can assess how radiation or drugs affect DNA damage and repair. The signal offers a molecular readout for comparing the extent of damage-associated responses under those experimental conditions. This makes it useful when investigating how treatments influence genome stability in biological systems and when evaluating treatment-related cellular responses.
γ-H2AX measurements support cancer biology studies and the development of DNA damage-based therapies. They connect treatment-related DNA damage and repair measurements with questions about genome stability, helping researchers evaluate biological responses relevant to therapeutic design. The marker therefore serves both as a research readout and as context for studying treatment strategies.