News and Views
Nature Structural & Molecular Biology 15, 542 - 544 (2008)
doi:10.1038/nsmb0608-542
Simplifying a complex code
Bryan M Turner1
-
Bryan M. Turner is at the Institute of Biomedical Research, University of Birmingham Medical School, Birmingham B15 2TT, UK.
e-mail: b.m.turner@bham.ac.uk
Abstract
Methylated lysines are essential components of the network of histone modifications, or 'histone code', that regulates gene expression. Work on the methyltransferase Dot1 shows how modifications on different histones interact to modulate activity and how its catalytic mechanism is matched to its role in genome regulation.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
Memorable transcriptionNature Cell Biology News and Views (01 May 2003)
Histone H3 Arg2 methylation provides alternative directions for COMPASSNature Structural & Molecular Biology News and Views (01 Nov 2007)
See all 3 matches for News And ViewsRESEARCH
Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation statesNature Structural & Molecular Biology Article (01 Jun 2008)
Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylationNature Letters to Editor (05 Jun 2008)
See all 53 matches for Research
