Video Experimental Relacionado
Updated: Jul 17, 2026
11:06
Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
Published on: December 29, 2017
La levadura Rtt109 promueve la estabilidad del genoma mediante la acetilación de la histona H3 en la lisina 56
Robert Driscoll1, Amanda Hudson, Stephen P Jackson
1Wellcome Trust and Cancer Research U.K. Gurdon Institute and the Department of Zoology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK.
Science (New York, N.Y.)
|February 3, 2007
Resumen
El estudio identifica a Saccharomyces cerevisiae Rtt109p como crucial para la estabilidad del genoma y la resistencia al daño del ADN. Rtt109p coopera con Asf1p para acetilizar la histona H3 en la lisina 56, esencial para la supervivencia celular durante la fase S.
Área de la Ciencia:
- Biología Molecular Biología Molecular
- Genética La genética.
- La bioquímica es la bioquímica.
Sus antecedentes:
- Las modificaciones postraslacionales de las histonas regulan las respuestas al daño del ADN.
- Las histonas acompañantes como Asf1p están involucradas en el mantenimiento de la cromatina.
- Comprender estos procesos es clave para la estabilidad del genoma.
Objetivo del estudio:
- Para investigar el papel de Saccharomyces cerevisiae Rtt109p en la respuesta al daño del ADN.
- Para aclarar el mecanismo por el cual funciona Rtt109p.
- Para identificar Rtt109p como una nueva histona acetiltransferasa.
Principales métodos:
- El análisis genético en Saccharomyces cerevisiae.
- Ensayos bioquímicos para estudiar la modificación de la histona.
- Experimentos in vivo e in vitro para evaluar la función de las proteínas.
Principales resultados:
- Rtt109p promueve la estabilidad del genoma y la resistencia a los agentes que dañan el ADN.
- Rtt109p coopera funcionalmente con la histona acompañante Asf1p.
- Rtt109p es necesario para y cataliza directamente la acetilación de la histona H3 en la lisina 56 (K56).
Conclusiones:
- Rtt109p es una nueva histona acetiltransferasa crítica para la respuesta al daño del ADN.
- La interacción Rtt109p-Asf1p es esencial para mantener la estructura de la cromatina y la supervivencia celular.
- Esta vía es vital para la resistencia celular al daño del ADN durante la fase S.
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...
01:53RNA Stability
Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
01:53RNA Stability
Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
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...