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1,2
* Cell Metabolism and Pharmacokinetics Laboratory, Regina Elena Cancer Institute, 00158 Rome, Italy;
Department of Experimental Medicine, University of LAquila, 67100 LAquila, Italy; and
Istituto di Tecnologie Biomediche, CNR, 00137 Rome, Italy
1Correspondence: Cell Metabolism and Pharmacokinetics Laboratory, Regina Elena Cancer Institute, Via Delle Messi doro 156, 00158 Rome, Italy. E-mail: fanciulli{at}crs.ifo.it; Istituto di Tecnologie Biomediche, CNR, Viale Marx 43, 00137 Rome, Italy. E-mail: passananti{at}itbm.rm.cnr.it
hRPB11 is a core subunit of RNA polymerase II (pol II) specifically
down-regulated on doxorubicin (dox) treatment. Levels of this protein
profoundly affect cell differentiation, cell proliferation, and
tumorigenicity in vivo. Here we describe Che-1, a novel
human protein that interacts with hRPB11. Che-1 possesses a domain of
high homology with Escherichia coli RNA polymerase
-factor 70 and SV40 large T antigen. In addition, we report that
Che-1 interacts with the retinoblastoma susceptibility gene (Rb) by two
distinct domains. Functionally, we demonstrate that Che-1 represses the
growth suppression function of Rb, counteracting the inhibitory action
of Rb on the trans-activation function of E2F1. These
results identify a novel protein that binds Rb and the core of pol II,
and suggest that Che-1 may be part of transcription regulatory
complex.Fanciulli, M., Bruno, T, Di Padova, M., De Angelis, R.,
Iezzi, S., Iacobini, C, Floridi, A., Passananti, C. Identification of a
novel partner of RNA polymerase II subunit 11, Che-1, which interacts
with and affects the growth suppression function of Rb.
Key Words: RNA polymerase II hRPB11 Che-1 Retinoblastoma susceptibility gene
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