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Structural basis for H3K4 trimethylation by yeast Set1/COMPASS
- Source :
- Advances in Enzyme Regulation. 50:104-110
- Publication Year :
- 2010
- Publisher :
- Elsevier BV, 2010.
-
Abstract
- Histone methylation on lysine 4 of histone H3 (H3K4) is a hallmark of activity of the transcribed regions on eukaryotic chromatin. H3K4 can be mono-, di- and trimethylated by Set1/COMPASS. In this review, we will discuss recent findings regarding the role of the Y/F switch by the catalytic domain of Set1 in the regulation of H3K4 methylation by Set1/COMPASS.
- Subjects :
- Models, Molecular
Cancer Research
Saccharomyces cerevisiae Proteins
animal structures
Protein Conformation
Saccharomyces cerevisiae
Biology
Methylation
environment and public health
Article
Histones
Histone H3
Histone H1
Histone H2A
Histone methylation
Genetics
Humans
Histone code
Histone octamer
Molecular Biology
Epigenomics
Lysine
Histone-Lysine N-Methyltransferase
Histone methyltransferase
Molecular Medicine
Subjects
Details
- ISSN :
- 00652571
- Volume :
- 50
- Database :
- OpenAIRE
- Journal :
- Advances in Enzyme Regulation
- Accession number :
- edsair.doi.dedup.....da7a258e557ae983ff38f1c80b7e96bb
- Full Text :
- https://doi.org/10.1016/j.advenzreg.2009.12.005