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Title: Hydroxymethyluracil DNA glycosylase in mammalian cells

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)

An activity has been purified 350-fold from extracts of mouse plasmacytoma cells that forms 5-hydroxymethyluracil (..cap alpha..-hydroxythymine) and apyrimidinic sites with phage SPO1 DNA, which contains this base in place of thymine. This DNA glycosylase presumably functions to eliminate hydroxymethyluracil, a major thymine-derived DNA lesion produced by ionizing radiation and oxidative damage. The enzyme has no cofactor requirement and is active in EDTA. Neither intermediate formation nor hydrolysis of hydroxymethyldeoxyuridine or hydroxymethyldeoxyuridine monophosphate was detected. The enzyme does not cleave apyrimidinic sites in DNA. It does release uracil from the uracil-containing DNA of phage PBS2, but this acitivity is less than 2% of the predominant uracil DNA glycosytase activity of the cell, which is separated by phosphocellulose chromatography. The major uracil DNA glycosylase does not release hydroxymethyluracil from SPO1 DNA. The hydroxymethyluracil glycosylase is also separated upon phosphocelluose chromatography from a thymine glycol DNA glycosylase activity that is accompanied by an apyrimidinic endonuclease activity. 33 references, 2 figures, 2 tables.

Research Organization:
Univ. of California, Berkeley, CA (United States)
OSTI ID:
5766088
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 81:13
Country of Publication:
United States
Language:
English