Partial purification of Pde1 from Saccharomyces cerevisiae: enzymatic redundancy for the repair of 3'-terminal DNA lesions and abasic sites in yeast

Biochemistry
M Sander, D Ramotar

Abstract

Earlier work indicates that the major DNA repair phosphodiesterase (PDE) in yeast cells is the well-characterized Apn1 protein. Apn1 demonstrates both Mg2+-independent PDE activity and Mg2+-independent class II apurinic/apyrimidinic (AP) endonuclease activity and represents greater than 90% of the activity detected in crude extracts from wild-type yeast cells. Apn1 is related to Echerichia coli endonuclease IV, both in its enzymatic properties and its amino acid sequence. In this work, we report the partial purification of a novel yeast protein, Pde1, present in Apn1-deficient cells. Pde1 is purified by sequential BioRex-70, PBE118, and MonoS chromatography steps using a sensitive and highly specific 3'-phosphoglycolate-terminated oligonucleotide-based assay as a measure of PDE activity. Mg2+-stimulated PDE and Mg2+-stimulated class II AP endonuclease copurify during this procedure. These results indicate that yeast, like many other organisms studied to date, has enzymatic redundancy for the repair of 3'-blocking groups and abasic sites.

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Citations

Dec 31, 2009·Nucleic Acids Research·Sylvia SteiningerSimone Moertl
Dec 1, 2001·American Journal of Respiratory Cell and Molecular Biology·Y H HeW J Martin
Jul 30, 2010·Mutation Research·James M DaleyDindial Ramotar
May 27, 2008·Fungal Genetics and Biology : FG & B·María D García-PedrajasMichael H Perlin
Dec 17, 2002·Oncogene·Bruce Demple, Michael S DeMott
Nov 24, 1998·Critical Reviews in Oral Biology and Medicine : an Official Publication of the American Association of Oral Biologists·M A Kukuruzinska, K Lennon
Jan 1, 1997·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·D Ramotar
Sep 20, 1997·The Journal of Biological Chemistry·Z WangE C Friedberg
Jul 9, 2014·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Kenneth C HessAntoni Barrientos

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