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Related Concept Videos

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...
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...
General Transcription Factors01:30

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...
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,...
Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the addition of a...

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Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
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Modulation of transcription factor function by O-GlcNAc modification.

Sabire Ozcan1, Sreenath S Andrali, Jamie E L Cantrell

  • 1Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536, USA. sozcan@uky.edu

Biochimica Et Biophysica Acta
|March 6, 2010
PubMed
Summary

O-linked beta-N-acetylglucosamine (O-GlcNAc) is a dynamic protein modification crucial for cellular processes. This review explores how O-GlcNAcylation impacts transcription factor function and its links to diseases like cancer and neurodegeneration.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • O-linked beta-N-acetylglucosamine (O-GlcNAc) is a dynamic post-translational modification found on nuclear and cytoplasmic proteins.
  • This modification plays a role in numerous cellular processes and is regulated by extracellular signals and metabolism.
  • Unlike protein phosphorylation, O-GlcNAc modification is catalyzed by a single enzyme, O-linked N-acetylglucosaminyl transferase (OGT), and removed by O-GlcNAcase (OGA).

Purpose of the Study:

  • To review the role of O-linked beta-N-acetylglucosamine (O-GlcNAc) modification in regulating transcription factor function.
  • To highlight the impact of O-GlcNAcylation on DNA binding, localization, stability, and transcriptional activity of transcription factors.
  • To discuss the implications of altered O-GlcNAc modification in various diseases, including cancer, diabetes, and neurodegeneration.

Main Methods:

  • Literature review focusing on studies investigating O-GlcNAc modification of transcription factors.
  • Analysis of research on the enzymes O-linked N-acetylglucosaminyl transferase (OGT) and O-GlcNAcase (OGA).
  • Synthesis of findings related to the functional consequences of O-GlcNAcylation on protein activity and disease pathogenesis.

Main Results:

  • O-GlcNAc modification dynamically regulates transcription factor activity, influencing their DNA binding, cellular localization, stability, and interactions with co-factors.
  • Dysregulation of O-GlcNAc levels is implicated in the development of diseases such as cancer, diabetes, cardiovascular disease, and neurodegenerative disorders.
  • The interplay between O-GlcNAc modification and other post-translational modifications, like phosphorylation, fine-tunes protein function.

Conclusions:

  • O-GlcNAc modification is a critical regulator of transcription factor function with significant implications for cellular homeostasis.
  • Understanding the role of O-GlcNAcylation in transcription factor regulation offers potential therapeutic targets for various diseases.
  • Further research into O-GlcNAc modification pathways is essential for deciphering complex biological processes and disease mechanisms.