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Papers In Press, published online ahead of print August 28, 2001
J. Biol. Chem, 10.1074/jbc.M106953200
Submitted on July 23, 2001
Revised on August 23, 2001
Accepted on August 27, 2001
Department of Pathology, Neww York University School of Medicine, New York, NY 10016
Corresponding Author: george.teebor{at}med.nyu.edu
Purification from calf thymus of a DNA N-glycosylase activity (HMUDG) that released 5-hydroxymethyluracil (5hmUra) from the DNA of B. subtilis phage SPO1 was undertaken. Analysis of the most purified fraction by SDS-PAGE revealed a multiplicity of protein species making it impossible to identify HMUDG by inspection. Therefore, we renatured the enzyme after SDS-PAGE and assayed slices of the gel for DNA N-glycosylase activity directed against 5hmUra. Maximum enzymatic activity was identified between MW markers 30 and 34 kD. Protein was extracted from gel slices and subjected to tryptic digestion and analysis by mass spectrometry. Analysis revealed the presence of 11 peptides which were homologous or identical to the sequence of human SMUG1, the recently characterized single stranded monofunctional uracil DNA N-glycosylase. The cDNA of hSMUG1 was isolated and expressed as a recombinant GST fusion protein, which was shown to release 5hmUra with 20 times the specific activity of the most purified bovine fraction. We conclude that hSMUG1 and HMUDG are the same protein.
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