News and Views
Nature Structural & Molecular Biology 14, 98 - 99 (2007)
doi:10.1038/nsmb0207-98
Tudor hooks up with DNA repair
Lorenzo Corsini1 & Michael Sattler1,2
- Lorenzo Corsini and Michael Sattler are at the European Molecular Biology Laboratory, Meyerhofstr. 1, D-69117 Heidelberg, Germany
- Michael Sattler is at the GSF-Research Center for Environment and Health, Ingolstädter, Landstr. 1, 85764, Neuherberg, Gemany and Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany. e-mail: sattler@embl.de
Abstract
Histone lysine methylation has a central role in transcriptional regulation and has recently been linked to DNA damage repair. Now it has been shown that the DNA damage repair factor 53BP1 is recruited to DNA double-strand breaks by its tandem tudor domain, which specifically recognizes histone H4 dimethylated at lysine 20.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Ankyrin for methylated lysinesNature Structural & Molecular Biology News and Views (01 Mar 2008)
Targeting the JMJD2A histone lysine demethylaseNature Structural & Molecular Biology News and Views (01 Aug 2007)
RESEARCH
L3MBTL1 recognition of mono- and dimethylated histonesNature Structural & Molecular Biology Brief Communication (01 Dec 2007)
Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1Oncogene Original Article
See all 16 matches for Research
