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p53 protein exhibits 3'-to-5' exonuclease activity

Authors :
Mummenbrauer, Torsten
Janus, Friedemann
Muller, Beate
Wiesmuller, Lisa
Deppert, Wolfgang
Grosse, Frank
Source :
Cell. June 28, 1996, Vol. 85 Issue 7, p1089, 11 p.
Publication Year :
1996

Abstract

The p53 protein shows exonuclease activity and degrades DNA with a 3'-to-5' polarity in the presence of Mg2+. The exonuclease activity is specific for the purified wild-type protein as p53 mutants lack the activity. The activity copurifies with p53 during the preparation of the wild-type protein but fails to copurify with mutant p53. The enzyme activity can be reconstituted from urea-denatured and SDS gel-purified p53 and mapped to the core region of the p53 molecule.

Details

ISSN :
00928674
Volume :
85
Issue :
7
Database :
Gale General OneFile
Journal :
Cell
Publication Type :
Academic Journal
Accession number :
edsgcl.18692443