Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains.
We have previously reported that Monad, a novel WD40 repeat protein, potentiates apoptosis induced by tumor necrosis factor-alpha(TNF-alpha) and cycloheximide (CHX). By affinity purification and mass spectrometry, we identified RNA polymerase II-associated protein 3 (RPAP3) as a binding protein of Monad. Overexpression of RPAP3 in HEK 293 potentiated caspase-3 activation and apoptosis induced by TNF-alpha and CHX. In addition, knockdown of RPAP3 by RNA interference resulted in a significant reduction of apoptosis induced by TNF-alpha and CHX in HEK293 and HeLa cells. These results raise the possibility that RPAP3, together with Monad, may function as a novel modulator of apoptosis pathway.
Department of Pharmacology, Graduate School of Dentistry, Osaka University, 1-8 Yamadaoka, Suita, Osaka 565-0871, Japan.
Yuki
Y
Itsuki
Makio
M
Saeki
Hirokazu
H
Nakahara
Hiroshi
H
Egusa
Yasuyuki
Y
Irie
Yutaka
Y
Terao
Shigetada
S
Kawabata
Hirofumi
H
Yatani
Yoshinori
Y
Kamisaki
D000595:Amino Acid Sequence; D017209:Apoptosis; D051017:Apoptosis Regulatory Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D002460:Cell Line; D003001:Cloning, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism; D020449:Repetitive Sequences, Amino Acid; D014018:Tissue Distribution
D051017:Apoptosis Regulatory Proteins; D002352:Carrier Proteins; C509833:DNAAF10 protein, human; D012333:RNA, Messenger; C472351:RPAP3 protein, human