Crystal structure of the human SUV39H1 chromodomain and its recognition of histone H3K9me2/3.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 23285239.
- Also identified by DOI 10.1371/journal.pone.0052977 and PMC identifier 3532415.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
SUV39H1, the first identified histone lysine methyltransferase in human, is involved in chromatin modification and gene regulation. SUV39H1 contains a chromodomain in its N-terminus, which potentially plays a role in methyl-lysine recognition and SUV39H1 targeting. In this study, the structure of the chromodomain of human SUV39H1 was determined by X-ray crystallography. The SUV39H1 chromodomain displays a generally conserved structure fold compared with other solved chromodomains. However, different from other chromodomains, the SUV39H1 chromodomain possesses a much longer helix at its C-terminus. Furthermore, the SUV39H1 chromodomain was shown to recognize histone H3K9me2/3 specifically.
Medical subject headings
- Histones
- Methyltransferases
- Repressor Proteins