Video Experimental Relacionado
Updated: May 9, 2026
08:12
Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
Published on: May 5, 2022
Una copia obtenida ilegalmente de un modificador de histonas gana ganancias
Ryan Rickels1, Ali Shilatifard
1Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA.
Cell
|August 6, 2013
Resumen
La sobreexpresión de la histona demetilasa causa ganancias temporales en copias genéticas específicas, lo que potencialmente conduce a la progresión del tumor. Este estudio arroja luz sobre los mecanismos moleculares detrás de las variaciones del número de copias (CNV) en el cáncer.
Área de la Ciencia:
- Genética La genética.
- Biología Molecular Biología Molecular
- Investigación del cáncer Investigación del cáncer.
Sus antecedentes:
- Los mecanismos moleculares subyacentes a las variaciones del número de copias específicas del sitio (CNVs) y su papel en la progresión tumoral siguen siendo en gran medida desconocidos.
- Comprender estos procesos es crucial para descifrar el desarrollo del cáncer.
Objetivo del estudio:
- Investigar la maquinaria molecular responsable de la inducción de las CNV específicas del sitio.
- Explorar el papel potencial de las CNV en la progresión cronológica de los tumores.
Principales métodos:
- El estudio se centró en los efectos de la sobreexpresión de una histona demetilasa específica.
- Investigó el impacto en los loci genómicos, particularmente aquellos que contienen proto-oncogenes.
Principales resultados:
- Se demostró que la sobreexpresión de la histona demetilasa induce una ganancia de copia transitoria en localizaciones genómicas específicas.
- Se sabe que estos loci objetivo albergan proto-oncogenes, lo que sugiere un vínculo directo.
Conclusiones:
- La actividad de la histona demetilasa puede influir directamente en la inestabilidad genómica mediante la inducción de CNVs.
- Este hallazgo proporciona un mecanismo molecular potencial que vincula las modificaciones epigenéticas al desarrollo temprano del tumor y la activación del proto-oncogén.
Videos de Conceptos Relacionados
02:32Histone Modification
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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:32Histone Modification
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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:25Spreading of Chromatin Modifications
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer is an enzyme that can...
Writers
The writer is an enzyme that can...
02:05Duplication of Chromatin Structure
The process of chromosome duplication during cell division requires genome-wide disruption and re-assembly of chromatin. The chromatin structure must be accurately inherited, reassembled, and maintained in the daughter cells to ensure lineage propagation.
The basic unit of the chromatin is the nucleosome, consisting of DNA wrapped around octameric histone proteins and short stretches of linker DNA separating individual nucleosomes. The histone proteins within the nucleosome have their...
The basic unit of the chromatin is the nucleosome, consisting of DNA wrapped around octameric histone proteins and short stretches of linker DNA separating individual nucleosomes. The histone proteins within the nucleosome have their...
01:32Chromatin Modification in iPS Cells
Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
02:30Histone Variants at the Centromere
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...