Related Experiment Video

Updated: Jul 4, 2026

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

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

Published on: December 26, 2020

[Histone-antihistone interactions in the Escherichia coli-Tetrahymena pyriformis association]

O V Bukharin, A O Plotnikov, N V Nemtseva

    Mikrobiologiia
    |June 5, 2008
    PubMed

    More Related Videos

    Investigating Interactions Between Histone Modifying Enzymes and Transcription Factors in vivo by Fluorescence Resonance Energy Transfer11:33

    Investigating Interactions Between Histone Modifying Enzymes and Transcription Factors in vivo by Fluorescence Resonance Energy Transfer

    Published on: October 14, 2022

    Chromatin Immunoprecipitation in the Cnidarian Model System Exaiptasia diaphana11:48

    Chromatin Immunoprecipitation in the Cnidarian Model System Exaiptasia diaphana

    Published on: March 17, 2023

    Related Concept Videos

    Position-effect Variegation02:32

    Position-effect Variegation

    In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
    Spreading of Chromatin Modifications02:25

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

    Stringent Response in E. coli

    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...
    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,...
    The Nucleosome Core Particle01:12

    The Nucleosome Core Particle

    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...