Video Experimental Relacionado
Updated: Jun 21, 2026
11:08
A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
La acetilación de lisina se dirige a los complejos proteicos y co-regula las principales funciones celulares
Chunaram Choudhary1, Chanchal Kumar, Florian Gnad
1Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
Science (New York, N.Y.)
|July 18, 2009
Resumen
La acetilación de lisina, una modificación proteica clave, fue analizada globalmente utilizando espectrometría de masas. Este estudio revela su amplio alcance regulatorio en los procesos celulares, comparable a otras modificaciones importantes.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Molecular Biología Molecular
- La proteómica es la proteómica.
Sus antecedentes:
- La acetilación de lisina es una modificación post-traducional reversible crucial que regula la expresión génica.
- Las limitaciones tecnológicas anteriores impidieron un análisis exhaustivo de sus funciones celulares.
Objetivo del estudio:
- Identificar y cuantificar globalmente los sitios de acetilación de lisina y sus cambios.
- Comprender las funciones celulares y el alcance regulatorio de la acetilación de lisina.
Principales métodos:
- Se empleó espectrometría de masas de alta resolución para identificar miles de sitios de acetilación de lisina.
- Se realizó un análisis cuantitativo de los cambios de acetilación utilizando inhibidores de la desacetilasa (SAHA y MS-275).
Principales resultados:
- Se identificaron 3600 sitios de acetilación de lisina en 1750 proteínas.
- Se ha demostrado la orientación preferencial de grandes complejos macromoleculares involucrados en la remodelación de la cromatina, el ciclo celular, el empalme, el transporte nuclear y la nucleación de actina.
- Se ha demostrado que la acetilación afecta a las interacciones 14-3-3 y regula la Cdc28.
Conclusiones:
- La acetilación de la lisina tiene un amplio alcance regulatorio, similar a otras modificaciones postraduccionales importantes.
- Este estudio proporciona una visión global de las funciones celulares de la acetilación de lisina, superando las barreras tecnológicas anteriores.
Más Videos Relacionados
12:49Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
14:32Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
Published on: February 27, 2016
Videos de Conceptos Relacionados
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
02:04Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
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,...
01:24Phase II Reactions: Acetylation Reactions
Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
02:04Co-activators and Co-repressors
Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...