HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Weger, S. Articles by Heilbronn, R. Search for Related Content PubMed PubMed Citation Articles by Weger, S. Articles by Heilbronn, R. Agricola Articles by Weger, S. Articles by Heilbronn, R.

Topors, a p53 and topoisomerase I binding protein, interacts with the adeno-associated virus (AAV-2) Rep78/68 proteins and enhances AAV-2 gene expression

Institut für Infektionsmedizin, Abteilung Virologie, Freie Universität Berlin, Hindenburgdamm 27, D-12203 Berlin, Germany¹

Author for correspondence: Regine Heilbronn. Fax +49 30 8445 4485. e-mail heilbronn{at}ukbf.fu-berlin.de

The adeno-associated virus type 2 (AAV-2) Rep proteins are essential for AAV DNA replication and regulation of AAV gene expression. We have identified a cellular protein interacting with Rep78 and Rep68 in yeast two-hybrid analysis and in GST pull-down assays. This protein has recently been described as both a p53 (p53BP3) and a topoisomerase I interacting protein (Topors). It contains an arginine/serine-rich domain, a RING finger domain and five PEST sequences. A minimal sequence sufficient for interaction with Rep was mapped to Topors amino acids 871 to 917. We show that the same region is also involved in the interaction with p53. Rep sequences involved in interaction with Topors were mapped to Rep amino acids 172 to 481. Overexpression of Topors stimulated AAV gene expression in the absence of helper virus, suggesting a function of Topors as a transcriptional regulator.

This article has been cited by other articles:

				K. Nash, W. Chen, M. Salganik, and N. Muzyczka Identification of Cellular Proteins That Interact with the Adeno-Associated Virus Rep Protein J. Virol., January 1, 2009; 83(1): 454 - 469. [Abstract] [Full Text] [PDF]

				C. Prives and E. White Does control of mutant p53 by Mdm2 complicate cancer therapy? Genes & Dev., May 15, 2008; 22(10): 1259 - 1264. [Abstract] [Full Text] [PDF]

				N. Lukashchuk and K. H. Vousden Ubiquitination and Degradation of Mutant p53 Mol. Cell. Biol., December 1, 2007; 27(23): 8284 - 8295. [Abstract] [Full Text] [PDF]

				J. M. Casper, J. M. Timpe, J. D. Dignam, and J. P. Trempe Identification of an Adeno-Associated Virus Rep Protein Binding Site in the Adenovirus E2a Promoter J. Virol., January 1, 2005; 79(1): 28 - 38. [Abstract] [Full Text] [PDF]

				R. Rajendra, D. Malegaonkar, P. Pungaliya, H. Marshall, Z. Rasheed, J. Brownell, L. F. Liu, S. Lutzker, A. Saleem, and E. H. Rubin Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53 J. Biol. Chem., August 27, 2004; 279(35): 36440 - 36444. [Abstract] [Full Text] [PDF]

				J. Secombe and S. M. Parkhurst Drosophila Topors Is a RING Finger-containing Protein That Functions as a Ubiquitin-protein Isopeptide Ligase for the Hairy Basic Helix-Loop-Helix Repressor Protein J. Biol. Chem., April 23, 2004; 279(17): 17126 - 17133. [Abstract] [Full Text] [PDF]

				D. F. Lackner and N. Muzyczka Studies of the Mechanism of Transactivation of the Adeno-Associated Virus p19 Promoter by Rep Protein J. Virol., July 17, 2002; 76(16): 8225 - 8235. [Abstract] [Full Text] [PDF]