Related Experiment Video

Updated: Aug 11, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

A specific lysine in c-Jun is required for transcriptional repression by E1A and is acetylated by p300

R G Vries1, M Prudenziati, C Zwartjes

  • 1Department of Molecular Cell Biology, Leiden University Medical Center, Wassenaarseweg 72, 2333 AL Leiden, The Netherlands.

The EMBO Journal
|November 2, 2001
PubMed

Insights

Adenovirus E1A protein represses transcription via p300/CBP coactivators. Specific repression of c-Jun involves acetylation at Lys271, essential for E1A

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Virology

Background:

  • Adenovirus E1A protein interacts with p300/CBP transcriptional coactivators.
  • E1A protein represses collagenase promoter activity activated by c-Jun.
  • E1A repression is specific and does not affect promoters activated by homologous factors like EB1.

Purpose of the Study:

  • To elucidate the mechanism of adenovirus E1A-mediated repression of c-Jun.
  • To identify the specific region and molecular modifications involved in E1A repression.

Main Methods:

  • Construction and analysis of c-Jun/EB1 chimera proteins.
  • Investigation of p300 acetyltransferase activity in E1A repression.
  • In vivo and in vitro acetylation assays of c-Jun.
  • Site-directed mutagenesis of c-Jun, focusing on Lys271.

Main Results:

  • A 12-amino acid region in the c-Jun basic region is critical for E1A repression.
  • c-Jun is acetylated in vivo, and Lys271 is essential for E1A-mediated repression.
  • Lys271 acetylation occurs both in vitro and in vivo, linking it to the repression mechanism.

Conclusions:

  • Adenovirus E1A specifically represses c-Jun-activated transcription.
  • Acetylation of c-Jun at Lys271 is a key step in E1A-mediated repression.
  • This study reveals a novel mechanism involving protein acetylation in viral gene regulation.

More Related Videos

Assays for Validating Histone Acetyltransferase Inhibitors09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently 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.
Histone Modification02:32

Histone 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,...
Co-activators and Co-repressors02:04

Co-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...
Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
Eukaryotic transcription inhibitors usually contain two distinct domains, a DNA...
Co-activators and Co-repressors02:04

Co-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...
Histone Modification02:32

Histone 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,...