Related Experiment Video
Updated: Jun 23, 2026
10:09
Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
Published on: January 26, 2018
LSD1 demethylates histone and non-histone proteins
Thomas B Nicholson1, Taiping Chen
1Developmental and Molecular Pathways, Novartis Institutes for Biomedical Research, Cambridge, MA 02139, USA.
Epigenetics
|April 28, 2009
Summary
Lysine-specific demethylase 1 (LSD1) removes methyl groups from histone proteins, impacting gene regulation and development. This enzyme also targets non-histone proteins, highlighting its broad biological significance.
Area of Science:
- Epigenetics and chromatin biology.
- Enzymology and protein regulation.
Background:
- Histone methylation is a key epigenetic modification regulating gene expression.
- Lysine-specific demethylase 1 (LSD1) was the first identified histone demethylase.
- LSD1 targets histone H3 on lysine 4 (H3K4) and lysine 9 (H3K9).
Purpose of the Study:
- To summarize the identification and known functions of Lysine-specific demethylase 1 (LSD1).
- To highlight LSD1's role in mammalian development and biological processes.
- To discuss LSD1's interactions with both histone and non-histone proteins.
Main Methods:
- Literature review of key studies on LSD1.
- Analysis of LSD1's enzymatic activity and substrate specificity.
- Examination of LSD1's protein domains and interaction partners.
Main Results:
- LSD1 is crucial for mammalian development.
- LSD1 demethylates histone H3K4 and H3K9.
- LSD1 also demethylates non-histone proteins like p53 and Dnmt1, regulating their functions.
- LSD1 functions through association with various protein complexes.
Conclusions:
- LSD1 plays a vital role in epigenetic regulation by modifying histone and non-histone proteins.
- LSD1's interactions with protein complexes are critical for its activity and specificity.
- Further research into LSD1 and its partners will illuminate its role in diverse biological processes.
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...
03:17Inheritance of Chromatin Structures
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 DNA...
01:32Chromatin Modification in iPS Cells
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...
02:38Heterochromatin
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...