Saeki, M (reprint author), Osaka Univ, Grad Sch Dent, Dept Pharmacol, 1-8 Yamadaoka, Suita, Osaka 5650871, Japan,email@example.com
We have previously reported that Monad, a novel WD40 repeat protein, potentiates apoptosis induced by tumor necrosis factor-a and cycloheximide. By affinity purification and mass spectrometry, RNA polymerase II-associated protein 3 (RPAP3) was identified as a Monad binding protein and may function with Monad as a novel modulator of apoptosis pathways. Here we report that Reptin, a highly conserved AAA + ATPase that is part of various chromatin-remodeling complexes, is also involved in the association of RPAP3 by immunoprecipitation and confocal microscopic analysis. Overexpression of RPAP3 induced HEK293 cells to death after UV-irradiation. Loss of RPAP3 by RNAi improved HeLa cell survival after UV-induced DNA damage and attenuated the phosphorylation of H2AX. Depletion of Reptin reduced cell survival and facilitated the phosphorylation on H2AX. These results suggest that RPAP3 modulates UV-induced DNA damage by regulating H2AX phosphorylation. J. Cell. Biochem. 106: 920-928, 2009. (C) 2009 Wiley-Liss, Inc.
Ni, Lin; Saeki, Makio; Xu, Li; Nakahara, Hirokazu; Saijo, Masafumi; Tanaka, Kiyoji; Kamisaki, Yoshinori.RPAP3 Interacts With Reptin to Regulate UV-Induced Phosphorylation of H2AX and DNA Damage,JOURNAL OF CELLULAR BIOCHEMISTRY,2009,106(5):920-928