Literature DB >> 6269847

Localization of the phosphoester bond hydrolyzed by the major apurinic/apyrmidinic endodeoxyribonuclease from rat-liver chromatin.

W G Verly, P Colson, G Zocchi, C Goffin, M Liuzzi, G Buchsenschmidt, M Muller.   

Abstract

The major apurinic/apyrimidinic (AP) endodeoxyribonuclease from rat liver chromatin, an enzyme specific for AP sites in DNA, cleaves the phosphodiester bridge which is the immediate neighbour of the AP site on its 5' side leaving 3'-hydroxyl and 5'-phosphate ends. In contrast with Escherichia coli endonuclease VI, this chromatin enzyme is inactive on reduced AP sites.

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Year:  1981        PMID: 6269847     DOI: 10.1111/j.1432-1033.1981.tb05505.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  1 in total

1.  An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro.

Authors:  Arnaud Hecker; Nicolas Leulliot; Danièle Gadelle; Marc Graille; Anthony Justome; Pierre Dorlet; Céline Brochier; Sophie Quevillon-Cheruel; Eric Le Cam; Herman van Tilbeurgh; Patrick Forterre
Journal:  Nucleic Acids Res       Date:  2007-08-30       Impact factor: 16.971

  1 in total

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