Changes in CTBP2 corepressor complex induced by E1A and modulation of E1A transcriptional activity by CTBP2

doi:10.1074/jbc.M603550200

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Papers In Press, published online ahead of print October 4, 2006
J. Biol. Chem, 10.1074/jbc.M603550200
Submitted on April 12, 2006
Revised on September 29, 2006
Accepted on October 4, 2006

Changes in CTBP2 corepressor complex induced by E1A and modulation of E1A transcriptional activity by CTBP2

Ling-Jun Zhao, T. Subramanian, and G. Chinnadurai

Institute for Molecular Virology, Saint Louis University Medical Center, St. Louis, MO 63110

Corresponding Author: chinnag{at}slu.edu

The N-terminal region of adenovirus E1A interacts with histone acetyl transferases (HATs) such as p300, P/CAF and GCN5. The C-terminal region interacts with the transcriptional corepressors CtBP1 and CtBP2. The functional significance of co-recruitment of HATs and CtBPs by E1A is not well understood. In this study, we have shown that E1A enhanced acetylation of CtBP2 by recruitment of p300 to the CtBP2 complex. Additionally, E1A also displaced the histone methyltransferase G9a and the E-box repressor ZEB from the CtBP2 complex through the C-terminal CtBP-binding domain. A transcriptional activation function encoded by the E1A N-terminal region was efficiently inhibited by CtBP2 but not by a mutant with an N-terminal deletion or by a mutant deficient in interaction with E1A. Two isoforms of CtBP1 (CtBP1-L and CtBP1-S) poorly inhibited transcriptional activity of the E1A N-terminal region. Thus, the N-terminal domain of CtBP2 may contribute a unique transcriptional regulatory activity of CtBP2. Our results provide new insights by which CtBP might modulate the biochemical activities of E1A.

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