Ontology highlight
ABSTRACT:
SUBMITTER: Hillringhaus L
PROVIDER: S-EPMC3308871 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature
Hillringhaus Lars L Yue Wyatt W WW Rose Nathan R NR Ng Stanley S SS Gileadi Carina C Loenarz Christoph C Bello Simon H SH Bray James E JE Schofield Christopher J CJ Oppermann Udo U
The Journal of biological chemistry 20110913 48
N(ε)-Methylations of histone lysine residues play critical roles in cell biology by "marking" chromatin for transcriptional activation or repression. Lysine demethylases reverse N(ε)-methylation in a sequence- and methylation-selective manner. The determinants of sequence selectivity for histone demethylases have been unclear. The human JMJD2 (KDM4) H3K9 and H3K36 demethylases can be divided into members that act on both H3K9 and H3K36 and H3K9 alone. Kinetic, crystallographic, and mutagenetic s ...[more]