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Related Concept Videos

Covalently Linked Protein Regulators02:04

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.
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...
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...

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Assays for Validating Histone Acetyltransferase Inhibitors
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Androgen receptor acetylation sites differentially regulate gene control.

Hortensia Faus1, Bernard Haendler

  • 1Therapeutic Research Group Oncology, Bayer Schering Pharma AG, D-13342 Berlin, Germany.

Journal of Cellular Biochemistry
|November 21, 2007
PubMed
Summary

Androgen receptor (AR) acetylation, a key post-translational modification, fine-tunes androgen-dependent gene responses. Mutating AR acetylation sites impacts potency and efficacy, showing promoter-selective effects crucial for gene regulation.

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Area of Science:

  • Molecular Biology
  • Endocrinology
  • Genetics

Background:

  • Androgen receptor (AR) function is regulated by post-translational modifications.
  • Acetylation is one such modification, occurring at specific lysine residues in the AR hinge domain.

Purpose of the Study:

  • To evaluate the role of AR acetylation in modulating androgen-dependent gene transcription.
  • To compare the activity of wild-type AR with AR mutated at acetylation sites on different promoters.

Main Methods:

  • Site-directed mutagenesis of AR acetylation sites.
  • Reporter gene assays to measure AR activity on natural and synthetic promoters (PSA, MMTV, Pem).
  • Subcellular localization studies and plasmid immunoprecipitation to assess AR translocation and promoter binding.

Main Results:

  • Mutation of AR acetylation sites altered the potency and efficacy of androgen response.
  • AR acetylation mutants showed promoter-selective effects, with reduced activity on the Pem promoter compared to PSA and MMTV.
  • Mutated and wild-type AR translocated similarly into the nucleus and bound comparably to the Pem promoter.

Conclusions:

  • AR acetylation plays a critical role in fine-tuning androgen-dependent gene expression.
  • The effects of AR acetylation are promoter-specific, highlighting its importance in regulating distinct target genes.
  • AR acetylation is independent of N/C-terminal interactions.