TY - JOUR
T1 - Functional interaction of the subunit 3 of RNA polymerase II (RPB3) with transcription factor-4 (ATF4)
AU - De Angelis, Roberta
AU - Iezzi, Simona
AU - Bruno, Tiziana
AU - Corbi, Nicoletta
AU - Di Padova, Monica
AU - Floridi, Aristide
AU - Fanciulli, Maurizio
AU - Passananti, Claudio
PY - 2003/7/17
Y1 - 2003/7/17
N2 - RPB3 is a core subunit of RNA polymerase II (pol II) that, together with the RPB11 subunit, forms the heterodimer considered as a functional counterpart of the bacterial α subunit homodimer involved in promoter recognition. We previously employed the yeast two-hybrid system and identified an interaction between RPB3 and the myogenic transcription factor myogenin, demonstrating an involvement of this subunit in muscle differentiation. In this paper we report the interaction between RPB3 and another known transcription factor, ATF4. We found that the intensity of the interaction between RPB3 and ATF4 is similar to the one between RPB3 and myogenin. This interaction involves an RPB3 specific region not homologous to the prokaryotic α subunit. We demonstrated that RBP3 is able to enhance ATF4 transactivation, whereas the region of RPB3 (Sud) that contacts ATF4, when used as a dominant negative, markedly inhibits ATF4 transactivation activity. Interestingly, ATF4 protein level, as reported for its partner RPB3, increases during C2C7 cell line muscle differentiation.
AB - RPB3 is a core subunit of RNA polymerase II (pol II) that, together with the RPB11 subunit, forms the heterodimer considered as a functional counterpart of the bacterial α subunit homodimer involved in promoter recognition. We previously employed the yeast two-hybrid system and identified an interaction between RPB3 and the myogenic transcription factor myogenin, demonstrating an involvement of this subunit in muscle differentiation. In this paper we report the interaction between RPB3 and another known transcription factor, ATF4. We found that the intensity of the interaction between RPB3 and ATF4 is similar to the one between RPB3 and myogenin. This interaction involves an RPB3 specific region not homologous to the prokaryotic α subunit. We demonstrated that RBP3 is able to enhance ATF4 transactivation, whereas the region of RPB3 (Sud) that contacts ATF4, when used as a dominant negative, markedly inhibits ATF4 transactivation activity. Interestingly, ATF4 protein level, as reported for its partner RPB3, increases during C2C7 cell line muscle differentiation.
KW - ATF4
KW - Muscle differentiation
KW - RNA polymerase II
KW - RPB3
UR - http://www.scopus.com/inward/record.url?scp=0038643841&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0038643841&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(03)00659-8
DO - 10.1016/S0014-5793(03)00659-8
M3 - Article
C2 - 12860379
AN - SCOPUS:0038643841
VL - 547
SP - 15
EP - 19
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-3
ER -