Related Experiment Video
Updated: Jul 2, 2025
09:46
Accessing the Cytotoxicity and Cell Response to Biomaterials
Published on: July 8, 2021
3.7K
Histone-modifying enzymes: Roles in odontogenesis and beyond
Yiting Li1, Pengcheng He1, Liwei Zheng1
1State Key Laboratory of Oral Diseases & National Center for Stomatology & National Clinical Research Center for Oral Diseases & Department of Pediatric Dentistry, West China Hospital of Stomatology, Sichuan University, Chengdu, Sichuan, China.
Oral Diseases
|February 20, 2024
Summary
Histone modifications are crucial for tooth development (odontogenesis). Disruptions in these epigenetic processes can lead to dental developmental diseases, highlighting their importance.
Area of Science:
- Developmental Biology
- Epigenetics
- Molecular Biology
Background:
- Tooth development (odontogenesis) involves complex epithelium-mesenchyme interactions.
- Epigenetic modifications, particularly histone modification, play a spatiotemporal role in tooth development.
- The specific roles and expression of histone-modifying enzymes during odontogenesis remain underexplored.
Purpose of the Study:
- To systematically review histone-modifying enzymes involved in odontogenesis.
- To elucidate the regulatory mechanisms of these enzymes during tooth development.
- To provide a theoretical basis for managing dental developmental diseases.
Main Methods:
- Systematic literature search of PubMed and Web of Science.
- Keywords used: "odontogenesis," "histone modification," and "enzyme."
Main Results:
- Histone modification is integral to the regulation of odontogenesis.
- Aberrant histone modifications can disrupt normal tooth development processes.
Conclusions:
- Histone modifications are critical regulators of tooth development.
- Further research is needed to understand downstream effects and therapeutic potential.
- Histone modifications represent a key area for studying tooth development and regeneration.
Related Concept Videos
02:32Histone Modification
13.3K
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...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
13.3K
02:25Spreading of Chromatin Modifications
8.3K
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...
Writers
The writer...
8.3K
01:12The Nucleosome Core Particle
915
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...
915
01:32Chromatin Modification in iPS Cells
1.7K
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.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
1.7K
02:54Nucleosome Remodeling
9.1K
Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
9.1K
03:17Inheritance of Chromatin Structures
6.2K
Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
6.2K