Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Covalently Linked Protein Regulators

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 Modification

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 Modification

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 Modifications

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...

Regulation of Nuclear Protein Sorting

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...

General Transcription Factors

General Transcription Factors

Tissue-specific transcription factors contribute to diverse cellular functions in mammals. For example, the gene for beta globin, a major component of hemoglobin, is present in all cells of the body. However, it is only expressed in red blood cells because the transcription factors that can bind to the promoter sequences of the beta globin gene are only expressed in these cells. Tissue-specific transcription factors also ensure that mutations in these factors may impair only the function of...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Temporary Interruption versus Continuation of Non-aspirin, Non-P2Y12 Antiplatelet Monotherapy for Delayed Post-polypectomy Bleeding.

Endoscopy international open·2026

Same author

Identification and characterization of a novel Plakoglobin-binding protein highly expressed in the testes.

Biochimica et biophysica acta. Molecular cell research·2026

Same author

Current status of split liver transplantation using machine perfusion in the United States.

HPB : the official journal of the International Hepato Pancreato Biliary Association·2026

Same author

[Effect of Implementing a General Imaging Management System on Promoting Medical Safety].

Nihon Hoshasen Gijutsu Gakkai zasshi·2026

Same author

β-Nicotinamide mononucleotide preserves muscle strength in septic male mice.

Scientific reports·2026

Same author

Clinical impact of butterbur shoot extract in dogs with oral melanoma: a combined phase 1 and 2 clinical trial.

BMC veterinary research·2026

Search research articles

Related Experiment Video

Updated: May 31, 2026

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

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

Published on: May 5, 2022

Multiple post-translational modifications in hepatocyte nuclear factor 4α.

Atsushi Yokoyama¹, Shogo Katsura, Ryo Ito

¹Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.

Biochemical and Biophysical Research Communications

|June 29, 2011

Summary

This summary is machine-generated.

This study reveals new post-translational modifications (PTMs) in hepatocyte nuclear factor 4α (HNF4α), uncovering a key acetylation site at lysine 458 that significantly impacts its transcriptional activity. Acetylation negatively regulates HNF4α, with implications for nutrient-responsive gene expression.

More Related Videos

Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog

Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog

Published on: November 5, 2014

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Related Experiment Videos

Last Updated: May 31, 2026

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

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

Published on: May 5, 2022

Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog

Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog

Published on: November 5, 2014

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Hepatocyte nuclear factor 4α (HNF4α) is a crucial transcription factor regulating genes involved in liver function and metabolism.
Post-translational modifications (PTMs) are known to modulate protein function, but their specific roles in HNF4α activity are not fully understood.

Purpose of the Study:

To comprehensively identify and characterize PTMs on HNF4α.
To investigate the functional impact of identified PTMs on HNF4α-mediated transcription.
To explore the regulatory role of HNF4α acetylation in response to nutrient availability.

Main Methods:

Mass spectrometry was employed for a comprehensive survey of PTMs in HNF4α.
Site-directed mutagenesis was used to create point mutations at identified PTM sites.
Transcriptional activity assays were performed to assess the functional consequences of PTMs.

Main Results:

Eight PTM sites on HNF4α were identified, including novel ubiquitination and acetylation sites.
Acetylation at lysine 458 was found to be a critical regulator of HNF4α transcriptional activity.
An acetylation-deficient mutant at K458 exhibited a two-fold increase in transcriptional activity, while an acetylation-mimicking mutant showed reduced activity.
HNF4α acetylation levels fluctuated in response to extracellular nutrient conditions.

Conclusions:

This study identified multiple novel PTMs on HNF4α, expanding the understanding of its regulatory landscape.
Acetylation at lysine 458 plays an unexpected inhibitory role in HNF4α-mediated transcription.
HNF4α acetylation is dynamically regulated by nutrient status, suggesting a mechanism for metabolic control.