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Proteomic characterization of novel histone post-translational modifications
Anna M Arnaudo1, Benjamin A Garcia
1Epigenetics Program, Department of Biochemistry and Biophysics, Perelman School of Medicine University of Pennsylvania, 1009C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, PA 19104, USA. bgarci@mail.med.upenn.edu.
Epigenetics & Chromatin
|August 7, 2013
Summary
Histone post-translational modifications (PTMs) are crucial in biology and disease. Recent advances in proteomic tools have expanded the understanding of histone PTMs and their functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Epigenetics
Background:
- Histone post-translational modifications (PTMs) play vital roles in biological processes and disease.
- Characterizing these modifications is essential for understanding cellular functions.
- The histone code, representing the combinatorial patterns of PTMs, is continuously expanding.
Purpose of the Study:
- To review proteomic tools for identifying and characterizing histone PTMs.
- To provide an overview of novel histone PTMs discovered in the last five years.
- To highlight advancements in probing PTM function.
Main Methods:
- Mass spectrometry is a key technique for histone PTM identification and validation.
- Development of novel proteomic tools aids in PTM discovery.
- Genomic and chemical biology approaches are used to investigate PTM function.
Main Results:
- Numerous novel histone PTM sites and types have been identified recently.
- These discoveries have significantly expanded the known histone code.
- New tools have enabled deeper insights into the functional roles of PTMs.
Conclusions:
- Proteomic tools are indispensable for advancing histone PTM research.
- Recent discoveries have broadened our understanding of epigenetic regulation.
- Continued development of innovative tools will further elucidate PTM functions in health and disease.
Related Concept Videos
02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:25Spreading 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...
Writers
The writer is an enzyme that can...
02:30Histone Variants at the Centromere
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...
02:04Covalently 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.
These groups modify specific amino acids in a protein.
01:12The Nucleosome Core Particle
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...