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| p53 protein exhibits 3'-to-5' exonuclease activity |
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| Author(s): Mummenbrauer T, Janus F, Muller B, Wiesmuller L, Deppert W, Grosse F |
| Source: CELL Volume: 85 Issue: 7 Pages: 1089-1099 Published: JUN 28 1996 |
| Times Cited: 200 References: 82 |
| Abstract: Highly purified p53 protein from different sources was able to degrade DNA with a 3'-to-5' polarity, yielding deoxynucleoside monophosphates as reaction products. This exonuclease activity was dependent on Mg2+ and inhibited by addition of 5 mM nucleoside monophosphates. This exonuclease activity is intrinsic to the wild-type p53 protein: it copurified with p53 during p53 preparation; only purified wild-type p53, but not identically purified mutant p53 proteins displayed exonuclease activity; the exonuclease activity could be reconstituted from SDS gel-purified and urea-renatured p53 protein and mapped to the core domain of the p53 molecule; and finally, purified p53 protein could be UV cross-linked to GMP. A p53-intrinsic exonuclease activity should substantially extend our view on the role of p53 as a ''guardian of the genome.'' |
| Document Type: Article |
| Language: English |
| Reprint Address: Mummenbrauer, T (reprint author), UNIV HAMBURG, HEINRICH PETTE INST EXPTL VIROL & IMMUNOL, MARTINISTR 52, D-20251 HAMBURG, GERMANY |
Addresses:
1. INST MOL BIOTECHNOL, BIOCHEM ABT, D-07745 JENA, GERMANY |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: UV484 |
| ISSN: 0092-8674 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |