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Related Concept Videos

Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

411
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...
411
Stringent Response in E. coli01:23

Stringent Response in E. coli

71
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
71
Metabolic States of the Body: Fasting and Starvation01:24

Metabolic States of the Body: Fasting and Starvation

1.9K
During the initial hours of fasting, the body uses up its glycogen stores as an energy source. Once these glycogen reserves are depleted, the body begins breaking down stored triglycerides and structural proteins. During this stage, glycerol becomes a key substrate for gluconeogenesis, while free fatty acids undergo beta-oxidation to provide energy for tissues, such as skeletal muscle. In the fasting state, the body spares protein breakdown as much as possible to conserve muscle and structural...
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Histone Modification02:32

Histone Modification

14.5K
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...
14.5K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.7K
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....
7.7K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.6K
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...
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Related Experiment Video

Updated: Oct 6, 2025

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

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Shifting acetylation during starvation.

Wei Wong1

  • 1Science Signaling, AAAS, Washington, DC 20005, USA.

Science Signaling
|January 18, 2022
PubMed
Summary

Yeast cells alter histone acetylation during glucose deprivation to boost acetyl-CoA production. This metabolic shift supports cellular energy needs under nutrient stress.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Glucose is a primary energy source for yeast.
  • Metabolic stress, like glucose deprivation, triggers cellular adaptations.
  • Histone acetylation regulates gene expression and metabolic pathways.

Purpose of the Study:

  • To investigate the role of histone acetylation in yeast metabolic adaptation to glucose deprivation.
  • To identify specific targets of histone acetylation during nutrient stress.

Main Methods:

  • Yeast culture under varying glucose conditions.
  • Chromatin immunoprecipitation sequencing (ChIP-seq) to analyze histone acetylation.
  • Quantitative PCR and Western blotting to validate gene expression changes.

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

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Using Microtiter Dish Radiolabeling for Multiple In Vivo Measurements Of Escherichia coli pppGpp Followed by Thin Layer Chromatography
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Using Microtiter Dish Radiolabeling for Multiple In Vivo Measurements Of Escherichia coli pppGpp Followed by Thin Layer Chromatography

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Related Experiment Videos

Last Updated: Oct 6, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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Main Results:

  • Glucose deprivation significantly altered histone acetylation patterns across the yeast genome.
  • Specific histone marks were enriched at genes involved in acetyl-CoA metabolism.
  • Increased acetylation correlated with upregulated expression of key enzymes in acetyl-CoA production.

Conclusions:

  • Histone acetylation is a key regulatory mechanism enabling yeast to adapt to glucose scarcity.
  • Redirected histone acetylation promotes acetyl-CoA synthesis, supporting cellular functions under stress.