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Related Concept Videos

Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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,...
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,...
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...
Nuclear Export01:42

Nuclear Export

The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...

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Related Experiment Video

Updated: Jun 16, 2026

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

HMG modifications and nuclear function.

Qingchun Zhang1, Yinsheng Wang

  • 1Department of Chemistry, University of California, Riverside, CA 92521-0403, USA.

Biochimica Et Biophysica Acta
|February 4, 2010
PubMed
Summary
This summary is machine-generated.

High mobility group (HMG) proteins regulate gene transcription and cellular processes. Chemical modifications to these proteins significantly impact their DNA interactions and biological functions within the nucleus.

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Measurement of Heme Synthesis Levels in Mammalian Cells
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Last Updated: Jun 16, 2026

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Protein Chemistry

Background:

  • High mobility group (HMG) proteins are crucial regulators of chromatin dynamics and gene transcription.
  • Post-translational modifications (PTMs) of HMG proteins can profoundly alter their DNA-binding affinities and protein-protein interactions.
  • Understanding the functional implications of HMG protein PTMs is essential for deciphering complex cellular regulatory networks.

Purpose of the Study:

  • To review the chemical modifications of mammalian High mobility group (HMG) proteins.
  • To elucidate the impact of these modifications on HMG protein functions.
  • To highlight the roles of modified HMG proteins in nuclear processes.

Main Methods:

  • Literature review focusing on mammalian HMG proteins.
  • Analysis of studies detailing post-translational modifications (PTMs) of HMG proteins.
  • Synthesis of current knowledge on HMG protein modification 'codes' and their functional consequences.

Main Results:

  • HMG proteins undergo diverse chemical modifications, including phosphorylation, acetylation, and ubiquitination.
  • These modifications dynamically regulate HMG protein interactions with DNA and other nuclear factors.
  • Specific modification patterns are linked to distinct roles in chromatin remodeling and transcriptional regulation.

Conclusions:

  • Post-translational modifications are key determinants of HMG protein function in mammalian cells.
  • The 'code' of HMG protein modifications provides critical insights into nuclear organization and gene expression.
  • Further research into HMG protein modification networks will advance our understanding of cellular regulation and disease.