JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ridgway, P J
Right arrow Articles by Braithwaite, A W
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ridgway, P J
Right arrow Articles by Braithwaite, A W

 Previous Article  |  Next Article 

J Virol. 1994 November; 68(11): 7178-7187

Functional characterization of Xenopus laevis p53: evidence of temperature-sensitive transactivation but not of repression.

P J Ridgway, T Soussi and A W Braithwaite

Division of Cell Biology, John Curtin School of Medical Research, Australian National University, Canberra.

ABSTRACT

We have investigated the effect of Xenopus laevis p53 (Xp53) on transcription from a variety of promoters which are regulated by mouse p53 using a chloramphenicol acetyltransferase reporter system. Although Xp53 transactivated promoters that are up-regulated by mouse p53, it was unable to cause repression. This ability to transactivate gene expression was dependent on a temperature of 32 degrees C, and activity was lost at 37 degrees C. Temperature-sensitive transactivation was correlated with temperature-dependent binding of Xp53 to the adenovirus E1B58K protein. Despite the marked loss of transcriptional activation and binding to E1B58K at 37 degrees C, Xp53 was still capable of binding simian virus 40 large T antigen and inhibiting simian virus 40 origin-dependent DNA replication. These data show that Xp53 is temperature sensitive for N-terminal activities and suggest that the transactivation and repression "domains" of p53 are distinct.


J Virol. 1994 November; 68(11): 7178-7187




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 1994 by the American Society for Microbiology. All rights reserved.