Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (423K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (9)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Melle, C.
Right arrow Articles by Nasheuer, H.-P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Melle, C.
Right arrow Articles by Nasheuer, H.-P.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2002, Vol. 30, No. 7 1493-1499
© 2002 Oxford University Press

Physical and functional interactions of the tumor suppressor protein p53 and DNA polymerase {alpha}-primase

Christian Melle and Heinz-Peter Nasheuer*

Institut für Molekulare Biotechnologie e.V., Abteilung Biochemie, Beutenbergstrasse 11, D-07745 Jena, Germany

The wild-type form of p53 contains an intrinsic 3'–5'-exonuclease activity. As p53 forms a complex with DNA polymerase {alpha}-primase (pol-prim) in vivo this finding suggests that p53 might cooperate with pol-prim to stabilize the genetic information of living cells. To test this hypothesis, exonuclease-free DNA pol-prim was expressed alone or together with p53 for purification. Pol-prim formed a complex with p53, which was purified by ion exchange and immunoaffinity chromatography from baculovirus-infected insect cells. The p53-containing pol-prim fractions removed a 3'-unpaired nucleotide with a 1.5–2-fold higher rate than a paired nucleotide, whereas the four subunit pol-prim did not have any exonuclase activity. Therefore, only p53/pol-prim was able to elongate a primer-template that contained a 3'-unpaired primer end in vitro. To achieve this, the 3'–5'-exonuclease activity of p53 excised the unpaired nucleotide at the 3'-end of the primer and created a paired 3'-end, which pol-prim was able to elongate. The exonuclease activity of p53 as well as the elongation of a primer with a mispaired 3'-end was inhibited specifically by the anti-p53 monoclonal antibodies PAb240 and PAb421.

* To whom correspondence should be addressed. Tel: +49 3641 656290; Fax: +49 3641 656288; Email: nasheuer{at}imb-jena.de Present address:Christian Melle, Institut für Humangenetik und Anthropologie, Friedrich-Schiller-Universität, Kollegiengasse 10, D-07740 Jena, Germany


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Antimicrob. Agents Chemother.Home page
M. Bakhanashvili, E. Novitsky, E. Rubinstein, I. Levy, and G. Rahav
Excision of Nucleoside Analogs from DNA by p53 Protein, a Potential Cellular Mechanism of Resistance to Inhibitors of Human Immunodeficiency Virus Type 1 Reverse Transcriptase
Antimicrob. Agents Chemother., April 1, 2005; 49(4): 1576 - 1579.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.