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SnapShot: Histone Lysine Methylase Complexes
- Source :
- Cell. (2):498-498.e1
- Publisher :
- Elsevier Inc.
-
Abstract
- adenosyl-L-methionine (SAM) to the e-amino group of a lysine residue on a histone to generate mono-, di-, and trimethylated histones. KMTs exist either singly or within complexes, in which the members of each complex modulate the activity of the enzymes. KMTs have been implicated in diverse roles in DNA-templated processes, and their mutations, deletions, or translocations have been linked with various human diseases. Known KMTs contain a SET domain (named after
- Subjects :
- Methyltransferase
animal structures
SET domain
viruses
Lysine
Chromosomal translocation
Biology
Histone-Lysine N-Methyltransferase
environment and public health
General Biochemistry, Genetics and Molecular Biology
03 medical and health sciences
0302 clinical medicine
030304 developmental biology
chemistry.chemical_classification
Genetics
0303 health sciences
Biochemistry, Genetics and Molecular Biology(all)
Lysine residue
3. Good health
enzymes and coenzymes (carbohydrates)
Enzyme
Histone
chemistry
Biochemistry
030220 oncology & carcinogenesis
biology.protein
health occupations
Subjects
Details
- Language :
- English
- ISSN :
- 00928674
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Cell
- Accession number :
- edsair.doi.dedup.....a737410ef7ad56905a5cd1c7601c45b5
- Full Text :
- https://doi.org/10.1016/j.cell.2012.03.025