Ontology highlight
ABSTRACT:
SUBMITTER: Cui G
PROVIDER: S-EPMC3454513 | biostudies-literature | 2012 Sep
REPOSITORIES: biostudies-literature
Cui Gaofeng G Park Sungman S Badeaux Aimee I AI Kim Donghwa D Lee Joseph J Thompson James R JR Yan Fei F Kaneko Satoshi S Yuan Zengqiang Z Botuyan Maria Victoria MV Bedford Mark T MT Cheng Jin Q JQ Mer Georges G
Nature structural & molecular biology 20120805 9
PHF20 is a multidomain protein and subunit of a lysine acetyltransferase complex that acetylates histone H4 and p53 but whose function is unclear. Using biochemical, biophysical and cellular approaches, we determined that PHF20 is a direct regulator of p53. A Tudor domain in PHF20 recognized p53 dimethylated at Lys370 or Lys382 and a homodimeric form of this Tudor domain could associate with the two dimethylated sites on p53 with enhanced affinity, indicating a multivalent interaction. Associati ...[more]