Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Videos de Conceptos Relacionados

The Nucleosome02:33

The Nucleosome

15.0K
DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
15.0K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

12.1K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
12.1K
Nucleosome Remodeling02:54

Nucleosome Remodeling

8.7K
Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
8.7K
The Nucleosome01:19

The Nucleosome

3.9K
Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
3.9K
Nucleic Acid Structure01:25

Nucleic Acid Structure

8.1K
The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA...
8.1K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.6K
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
2.6K

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

Structural and mechanistic studies on repair of 8-oxoguanine in mammalian cells.

Cold Spring Harbor symposia on quantitative biology·2003
Same author

Chemical communication across the zinc tetrathiolate cluster in Escherichia coli Ada, a metalloactivated DNA repair protein.

Biochemistry·2001
Same author

Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase.

The EMBO journal·2001
Same author

Coupling of substrate recognition and catalysis by a human base-excision DNA repair protein.

Journal of the American Chemical Society·2001
Same author

A synthetic library of cell-permeable molecules.

Journal of the American Chemical Society·2001
Same author

The synthesis of an exhaustively stereodiversified library of cis-1,5 enediols by silyl-tethered ring-closing metathesis.

Organic letters·2001

Video Experimental Relacionado

Updated: Apr 28, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

20.3K

Estructura de la solución del núcleo del complejo NFATC1/ADN.

P Zhou1, L J Sun, V Dötsch

  • 1Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

Cell
|March 20, 1998
PubMed
Resumen
Este resumen es generado por máquina.

El factor nuclear del dominio de unión al ADN de las células T activadas (NFAT) sufre cambios estructurales al unirse al ADN, lo que facilita la regulación génica. Esta flexibilidad estructural es clave para las interacciones de las proteínas y la transcripción génica.

Más Videos Relacionados

A Chromatin Immunoprecipitation Assay to Identify Novel NFAT2 Target Genes in Chronic Lymphocytic Leukemia
09:52

A Chromatin Immunoprecipitation Assay to Identify Novel NFAT2 Target Genes in Chronic Lymphocytic Leukemia

Published on: December 4, 2018

7.2K
Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques
05:58

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques

Published on: September 6, 2024

1.6K

Videos de Experimentos Relacionados

Last Updated: Apr 28, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
16:24

Analyzing and Building Nucleic Acid Structures with 3DNA

Published on: April 26, 2013

20.3K
A Chromatin Immunoprecipitation Assay to Identify Novel NFAT2 Target Genes in Chronic Lymphocytic Leukemia
09:52

A Chromatin Immunoprecipitation Assay to Identify Novel NFAT2 Target Genes in Chronic Lymphocytic Leukemia

Published on: December 4, 2018

7.2K
Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques
05:58

Author Spotlight: Efficient Nucleosome Reconstitution for Single-Molecule Techniques

Published on: September 6, 2024

1.6K

Área de la Ciencia:

  • Biología Molecular Biología Molecular
  • Biología Estructural Biología estructural.
  • Inmunología Inmunología.

Sus antecedentes:

  • Los factores de transcripción del factor nuclear de la célula T activada (NFAT) regulan la expresión génica de las citoquinas.
  • Las proteínas NFAT se unen a las regiones promotoras / potenciadoras de genes sensibles al antígeno, a menudo con otros socios de unión al ADN.

Objetivo del estudio:

  • Determinar la estructura de solución del complejo binario entre el dominio de unión de ADN NFATC1 humano y el sitio de ADN ARRE2.
  • Comprender cómo la unión al ADN influye en la estructura de NFAT y su papel en la regulación transcripcional.

Principales métodos:

  • Determinación de la estructura de la solución del dominio de unión al ADN NFATC1 / complejo de ADN ARRE2.
  • Análisis de los cambios estructurales inducidos por la unión al ADN.

Principales resultados:

  • Se aclaró la estructura del complejo binario NFATC1-ADN.
  • La unión al ADN induce el plegamiento de los elementos estructurales clave en NFATC1.1.
  • Estos elementos son cruciales para el reconocimiento de secuencias específicas de ADN y las interacciones proteína-proteína.
  • La orientación del dominio en el complejo binario difiere de la de un complejo ternario, lo que sugiere cambios conformacionales.

Conclusiones:

  • La unión al ADN induce reordenamientos estructurales significativos en el dominio de unión al ADN de NFAT.
  • Estas reorganizaciones son esenciales para la función de NFAT en la regulación génica.
  • NFAT puede reorientar su dominio de unión al ADN al formar complejos transcripcionales cooperativos.