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Related Concept Videos

Histone Modification02:32

Histone Modification

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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
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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.
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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.
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Phase II Reactions: Acetylation Reactions01:24

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Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
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Proteome-wide acetylation dynamics in human cells.

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This study reveals dynamic protein acetylation patterns using mass spectrometry. Metabolism influences acetylation rates, impacting protein function and cellular processes like chromatin and RNA metabolism.

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Area of Science:

  • Biochemistry
  • Proteomics
  • Molecular Biology

Background:

  • Protein acetylation is a crucial post-translational modification regulating protein function, stability, and localization.
  • Understanding protein acetylation dynamics is essential for deciphering its role in various biological processes.

Purpose of the Study:

  • To comprehensively characterize protein acetylation dynamics using a novel mass spectrometry-based proteomics approach.
  • To investigate the influence of cellular metabolism on protein acetylation rates and trends.

Main Methods:

  • Utilized stable isotope labeling with 13C-glucose or D3-acetate to trace acetyl-CoA metabolism and protein acetylation.
  • Employed mass spectrometry (MS) based proteomics to analyze protein acetylation across eight time points.
  • Developed a platform to monitor heavy acetyl incorporation rates and identify acetylation trends.

Main Results:

  • Identified approximately 1,000 acetylation sites with significant increasing acetylation trends.
  • Clustered acetylation sites based on their incorporation rates, revealing distinct functional enrichments.
  • Observed faster acetylation rates in chromatin and RNA metabolism proteins, and slower rates in lipid metabolism proteins.
  • Discovered acetylation sites with rapid catalysis, including on histone acetyltransferase p300, suggesting feedback regulation.

Conclusions:

  • Protein acetylation is a dynamic process significantly influenced by cellular metabolism.
  • Differential acetylation rates correlate with specific protein functions and metabolic pathways.
  • The findings provide insights into the regulatory mechanisms of protein acetylation, including potential feedback loops involving acetyltransferases.