Histone acetylation facilitates association of nucleosomes with SET domain of ALL-1 methyltransferase in vitro.
The inheritable methylation pattern of gene activity, created upon cell differentiation, is further maintained by the "SET" (methyltransferase)-domain proteins. However, it is still not clear how SET-proteins can decide on the required gene activity state and the way their chromatin association is maintained. Here we have found that high levels of histone acetylation--the hallmarks of active chromosome regions in vivo--can increase the affinity of reconstituted nucleosomes to the SET domain of ALL-1 histone methyltransferase in a defined system in vitro.
Krajewski
Wladyslaw A
WA
Institute of Developmental Biology of Russian Academy of Sciences, Moscow, Russia. wkrajewski@hotmail.com
Vassiliev
Oleg L
OL
D000107:Acetylation; D006367:HeLa Cells; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D051788:Myeloid-Lymphoid Leukemia Protein / Q000378:metabolism*; D009707:Nucleosomes / Q000201:enzymology*; D017434:Protein Structure, Tertiary
D006657:Histones; C497422:KMT2A protein, human; D009707:Nucleosomes; D051788:Myeloid-Lymphoid Leukemia Protein; D011495:Histone-Lysine N-Methyltransferase