Ontology highlight
ABSTRACT:
SUBMITTER: Colino-Sanguino Y
PROVIDER: S-EPMC6889796 | biostudies-literature | 2019 Nov
REPOSITORIES: biostudies-literature
Colino-Sanguino Yolanda Y Cornett Evan M EM Moulder David D Smith Grady C GC Hrit Joel J Cordeiro-Spinetti Eric E Vaughan Robert M RM Krajewski Krzysztof K Rothbart Scott B SB Clark Susan J SJ Valdés-Mora Fátima F
iScience 20191031
Acetylation of the histone variant H2A.Z (H2A.Zac) occurs at active regulatory regions associated with gene expression. Although the Tip60 complex is proposed to acetylate H2A.Z, functional studies suggest additional enzymes are involved. Here, we show that p300 acetylates H2A.Z at multiple lysines. In contrast, we found that although Tip60 does not efficiently acetylate H2A.Z in vitro, genetic inhibition of Tip60 reduces H2A.Zac in cells. Importantly, we found that interaction between the p300- ...[more]